NCBI Conserved Domain Search

Conserved domains on [gi|568981353|ref|XP_006516528|]

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aldo-keto reductase family 1, member C20 isoform X1 [Mus musculus]

Protein Classification

aldo/keto reductase( domain architecture ID 14442631)

aldo/keto reductase is a soluble NAD(P)(H) oxidoreductase that catalyzes the reduction of aldehydes and ketones to their corresponding primary and secondary alcohols

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

AKR_AKR1C1-35

cd19108

AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ...

6-286

0e+00

AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.

Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 630.42 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19108    1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108   81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 166 CNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMA 225
Cdd:cd19108  161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysalgsqrdkewVDQNSPVLLEDPVLCALA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 226 KKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 286
Cdd:cd19108  241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301

Name

Accession

Description

Interval

E-value

AKR_AKR1C1-35

cd19108

AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ...

6-286

0e+00

Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 630.42 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19108    1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108   81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 166 CNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMA 225
Cdd:cd19108  161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysalgsqrdkewVDQNSPVLLEDPVLCALA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 226 KKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 286
Cdd:cd19108  241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301

ARA1

COG0656

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...

12-285

3.06e-105

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 307.37 E-value: 3.06e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  12 DGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHR 91
Cdd:COG0656    1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  92 PELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRR 171
Cdd:COG0656   74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 172 QLEKILSKPGlkYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQV 241
Cdd:COG0656  134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCR-EHGIVVeaysplgrgkLLDDPVLAEIAEKHGKTPAQVVLRWHL 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568981353 242 QRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:COG0656  211 QRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254

dkgA

PRK11565

2,5-didehydrogluconate reductase DkgA;

5-268

4.25e-62

2,5-didehydrogluconate reductase DkgA;

Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 197.99 E-value: 4.25e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVL-LNDGHFIPILGFGT-SAPQEVPRSKATEAtkiaIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCT 82
Cdd:PRK11565   3 NPTVIkLQDGNVMPQLGLGVwQASNEEVITAIHKA----LEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  83 SKVWQTFHRPelVQVCLEQSLKQLQLDYVDLYLIHFPIAMKpgENYFpkdengkfiydavdicDTWEAMEKCKDAGLAKS 162
Cdd:PRK11565  75 TKLWNDDHKR--PREALEESLKKLQLDYVDLYLMHWPVPAI--DHYV----------------EAWKGMIELQKEGLIKS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 163 IGVCNFNRRQLEKILSKPGLkyKPVCNQVECHPYLNQRKLLDFCRVDK----SFPVL-------LDDPVLGSMAKKYNRT 231
Cdd:PRK11565 135 IGVCNFQIHHLQRLIDETGV--TPVINQIELHPLMQQRQLHAWNATHKiqteSWSPLaqggkgvFDQKVIRDLADKYGKT 212

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568981353 232 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQL 268
Cdd:PRK11565 213 PAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRL 249

Aldo_ket_red

pfam00248

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...

19-280

6.38e-54

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.

Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 177.50 E-value: 6.38e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   19 LGFGTSA----PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgTVKREDIFCTSKV------ 85
Cdd:pfam00248   1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248  77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  166 CNFNRRQLEKILSKPglKYKPVCNQVECHPY--LNQRKLLDFCRvDKSFPV----------------------------- 214
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCK-KNGIPLiaysplggglltgkytrdpdkgpgerrrl 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353  215 --------LLDDPVLGSMAKKYNRTPALIALRY--QVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:pfam00248 215 lkkgtplnLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290

Name

Accession

Description

Interval

E-value

AKR_AKR1C1-35

cd19108

AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ...

6-286

0e+00

Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 630.42 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19108    1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108   81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 166 CNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMA 225
Cdd:cd19108  161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKskdivlvaysalgsqrdkewVDQNSPVLLEDPVLCALA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 226 KKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 286
Cdd:cd19108  241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301

AKR_AKR1D1-3

cd19109

AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ...

13-299

2.45e-158

AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.

Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 443.86 E-value: 2.45e-158

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGT-SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHR 91
Cdd:cd19109    1 GNSIPIIGLGTySEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  92 PELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRR 171
Cdd:cd19109   81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 172 QLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR--------------------VDKSFPVLLDDPVLGSMAKKYNRT 231
Cdd:cd19109  161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQqhdivivaysplgtcrdpiwVNVSSPPLLEDPLLNSIGKKYNKT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568981353 232 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPF 299
Cdd:cd19109  241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308

AKR_AKR1A1-4

cd19106

AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ...

10-293

2.15e-128

AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.

Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 367.87 E-value: 2.15e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGT-VKREDIFCTSKVW 86
Cdd:cd19106    1 LHTGQKMPLIGLGTwkSKPGQV-----KAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19106   76 NTKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-------------------VDKSFPVLLDDPVLGSMAKK 227
Cdd:cd19106  156 NFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKarglvvtaysplgspdrpwAKPDEPVLLEEPKVKALAKK 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353 228 YNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISED 293
Cdd:cd19106  234 YNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVD 299

AKR_AKR1B1-19

cd19107

AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ...

16-303

1.34e-126

AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.

Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 363.28 E-value: 1.34e-126

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19107    4 MPILGLGT---WKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  96 QVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 175
Cdd:cd19107   81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 176 ILSKPGLKYKPVCNQVECHPYLNQRKLLDFCRV--------------DKSF-----PVLLDDPVLGSMAKKYNRTPALIA 236
Cdd:cd19107  161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSkgivvtaysplgspDRPWakpedPSLLEDPKIKEIAAKHNKTTAQVL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568981353 237 LRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPFLDEY 303
Cdd:cd19107  241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307

AKR_AKR1E1-2

cd19110

AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ...

16-303

3.41e-119

AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.

Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 344.25 E-value: 3.41e-119

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPE 93
Cdd:cd19110    4 IPAVGLGTwkASPGEV-----TEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  94 LVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQL 173
Cdd:cd19110   79 LVKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 174 EKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV--------LLDDPVLGSMAKKYNRTPALIALRYQ 240
Cdd:cd19110  159 ERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQsrnvsVTAYRPLggscegvdLIDDPVIQRIAKKHGKSPAQILIRFQ 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981353 241 VQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYIGSSISEDHPDFPFLDEY 303
Cdd:cd19110  239 IQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301

AKR_AKR2E1-5

cd19116

AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ...

7-286

2.82e-117

AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.

Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 339.26 E-value: 2.82e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGTSapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVW 86
Cdd:cd19116    2 TIKLNDGNEIPAIALGTW--KLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENyfpKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19116   80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSkpGLKYKPVCNQVECHPYLNQRKLLDFC--------------RVDKSF----PVLLDDPVLGSMAKKY 228
Cdd:cd19116  157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCqsngivvmayspfgRLVPRGqtnpPPRLDDPTLVAIAKKY 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568981353 229 NRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 286
Cdd:cd19116  235 GKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292

AKR_AKR1-5-like

cd19071

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...

16-277

5.86e-113

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.

Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 326.36 E-value: 5.86e-113

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVdgtvKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19071    1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGV----PREELFITTKLWPTDHGYERV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  96 QVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENyfpkdengkfiydAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 175
Cdd:cd19071   74 REALEESLKDLGLDYLDLYLIHWPVPGKEGGS-------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 176 ILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----------VDKSFPVLLDDPVLGSMAKKYNRTPALIALRYQVQRG 244
Cdd:cd19071  141 LLAAA--RIKPAVNQIELHPYLQQKELVEFCKehgivvqayspLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRG 218

                        250       260       270
                 ....*....|....*....|....*....|...
gi 568981353 245 VVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19071  219 VVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251

AKR_AKR3G1

cd19123

AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ...

7-286

1.41e-106

AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.

Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 312.04 E-value: 1.41e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSK 84
Cdd:cd19123    3 TLPLSNGDLIPALGLGTwkSKPGEV-----GQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  85 VWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGEnYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19123   78 LWNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 165 VCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR---------------------VDKSFPVLLDDPVLGS 223
Cdd:cd19123  157 VSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRdngihltaysplgsgdrpaamKAEGEPVLLEDPVINK 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981353 224 MAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRYI 286
Cdd:cd19123  235 IAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297

ARA1

COG0656

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...

12-285

3.06e-105

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 307.37 E-value: 3.06e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  12 DGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHR 91
Cdd:COG0656    1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  92 PELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRR 171
Cdd:COG0656   74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 172 QLEKILSKPGlkYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQV 241
Cdd:COG0656  134 HLEELLAETG--VKPAVNQVELHPYLQQRELLAFCR-EHGIVVeaysplgrgkLLDDPVLAEIAEKHGKTPAQVVLRWHL 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568981353 242 QRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:COG0656  211 QRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254

AKR_AKR1G1_CeAKR

cd19154

Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...

10-284

2.06e-103

Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.

Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 304.33 E-value: 2.06e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQ 87
Cdd:cd19154    6 LSNGVKMPLIGLGTwqSKGAEG-----ITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19154   81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-------------------VDKSF-----PVLLDDPVLGS 223
Cdd:cd19154  161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKkhnisvtsyatlgspgranFTKSTgvspaPNLLQDPIVKA 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 224 MAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIR 284
Cdd:cd19154  239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299

AKR_AKR4C1-15

cd19125

AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ...

10-279

6.76e-99

AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.

Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 292.33 E-value: 6.76e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGT--SAPqevprSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQ 87
Cdd:cd19125    5 LNTGAKIPAVGLGTwqADP-----GVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGEnyfPKDENGKFIydAVDICDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19125   80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV-----------LLDDPVLGSMAKKYNRT 231
Cdd:cd19125  155 FSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKskgihLSAYSPLgspgttwvkknVLKDPIVTKVAEKLGKT 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 232 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19125  233 PAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280

AKR_AKR1I_CgAKR1

cd19155

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ...

5-284

3.52e-92

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.

Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 275.94 E-value: 3.52e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCT 82
Cdd:cd19155    1 RNCVTFNNGEKMPVVGLGTwqSSPEEI-----ETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  83 SKVWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMK-PGENYFPKDENGKFIYD-AVDICDTWEAMEKCKDAGLA 160
Cdd:cd19155   76 TKLPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR--------------------------VDKSFPV 214
Cdd:cd19155  156 RSIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSthsitvtayaplgspgaahfspgtgsPSGSSPD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 215 LLDDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIR 284
Cdd:cd19155  234 LLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303

AKR_AKR3B1-3

cd19118

AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ...

10-265

1.93e-88

AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.

Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 265.43 E-value: 1.93e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIR-SKIVDGTVKREDIFCTSKVW 86
Cdd:cd19118    1 LNTGNKIPAIGLGTwqAEPGEV-----GAAVKIALKAGYRHLDLAKVYQNQHEVGQALKeLLKEEPGVKREDLFITSKLW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPK-----DENGKFIYDAVDICDTWEAMEKCKDAGLAK 161
Cdd:cd19118   76 NNSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavptNGGEVDLDLSVSLVDTWKAMVELKKTGKVK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 162 SIGVCNFNRRQLEKILSKPGLkyKPVCNQVECHPYLNQRKLLDFCRVDK--------------SFPVLLDDPVLGSMAKK 227
Cdd:cd19118  156 SIGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNihitaysplgnnlaGLPLLVQHPEVKAIAAK 233

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568981353 228 YNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFE 265
Cdd:cd19118  234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE 271

AKR_BaDH-like

cd19129

Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ...

11-263

8.43e-88

Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.

Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 264.32 E-value: 8.43e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  11 NDGHFIPILGFGTSAPQEvprSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFH 90
Cdd:cd19129    1 NGSGAIPALGFGTLIPDP---SATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  91 RPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYD-AVDICDTWEAMEKCKDAGLAKSIGVCNFN 169
Cdd:cd19129   78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDdGVTLLDTWRAMERLVDEGRCKAIGLSDVS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 170 RRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR----VDKSF--------PVLLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19129  158 LEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKnhgiVLQAFaplghgmePKLLEDPVITAIARRVNKTPAQVLL 235

                        250       260
                 ....*....|....*....|....*.
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQV 263
Cdd:cd19129  236 AWAIQRGTALLTTSKTPSRIRENFDI 261

AKR_AKR1G1_1I

cd19111

Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...

13-285

4.90e-87

Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.

Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 262.05 E-value: 4.90e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFH 90
Cdd:cd19111    1 GFPMPVIGLGTyqSPPEEV-----RAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  91 RPELVQVCLEQSLKQLQLDYVDLYLIHFPIamkpGENYfpKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNR 170
Cdd:cd19111   76 EFKDTEKSLEKSLENLKLPYVDLYLIHHPC----GFVN--KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 171 RQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFC-----------------RVDKSF----PVLLDDPVLGSMAKKYN 229
Cdd:cd19111  150 RQINKILAYA--KVKPSNLQLECHAYLQQRELRKFCnkknivvtayaplgspgRANQSLwpdqPDLLEDPTVLAIAKELD 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353 230 RTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19111  228 KTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283

AKR_AKR3A1-2

cd19117

AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ...

5-281

8.92e-87

AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.

Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 261.28 E-value: 8.92e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVLLNDGHFIPILGFGT--SAPQEVprSKATEAtkiAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCT 82
Cdd:cd19117    3 SKTFKLNTGAEIPAVGLGTwqSKPNEV--AKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFIT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  83 SKVWQTFHRPelVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPG--ENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19117   74 TKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEKILSKPGLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV------LLDDPVLGSMAKKYN 229
Cdd:cd19117  152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKskgihATAYSPLgstnapLLKEPVIIKIAKKHG 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568981353 230 RTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEfqLTSVDMKVLDGLNK 281
Cdd:cd19117  232 KTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKLFT--LSDEEFKEIDELHK 281

AKR_AKR4A_4B

cd19124

AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ...

12-279

7.87e-85

AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.

Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 256.04 E-value: 7.87e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  12 DGHFIPILGFGTSAPQEVPrSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVK-REDIFCTSKVWQTFH 90
Cdd:cd19124    1 SGQTMPVIGMGTASDPPSP-EDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  91 RPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENgkfIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNR 170
Cdd:cd19124   80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEE---DFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSC 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 171 RQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR----VDKSFPVL------------LDDPVLGSMAKKYNRTPAL 234
Cdd:cd19124  157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKangiHVTAYSPLgapgtkwgsnavMESDVLKEIAAAKGKTVAQ 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568981353 235 IALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19124  235 VSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279

AKR_AKR5C2

cd19131

Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...

7-280

1.46e-84

Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.

Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 254.60 E-value: 1.46e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW 86
Cdd:cd19131    1 TITLNDGNTIPQLGLGV---WQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKLW 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKpgenyfpkdenGKFIydavdicDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19131   74 NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-----------DKYV-------ETWKALIELKKEGRVKSIGVS 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSKPGLKykPVCNQVECHPYLNQRKLLDFC-----RVDKSFPV----LLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19131  136 NFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHakhgiQTESWSPLgqggLLSDPVIGEIAEKHGKTPAQVVI 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19131  214 RWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256

AKR_AKR3F2_3

cd19073

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...

16-277

7.03e-82

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.

Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 247.18 E-value: 7.03e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:cd19073    1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA----ESGVPREDLFITTKVWRDHLRPEDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  96 QVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 175
Cdd:cd19073   74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 176 ILSKPGLKykPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQVQRGVV 246
Cdd:cd19073  135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRendivITAYSPLargeVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIV 212

                        250       260       270
                 ....*....|....*....|....*....|.
gi 568981353 247 VLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19073  213 VIPKASSEDHLKENLAIFDWELTSEDVAKID 243

AKR_AKR5G1-3

cd19157

AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...

7-285

1.01e-81

AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.

Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 247.69 E-value: 1.01e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGTSAPQEvpRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDgtvkREDIFCTSKVW 86
Cdd:cd19157    1 TVTLNNGVKMPWLGLGVFKVEE--GSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIP----REELFITSKVW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIamkpgenyfpkdeNGKFIydavdicDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19157   75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPV-------------KGKYK-------ETWKALEKLYKDGRVRAIGVS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19157  135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKkqgiqLEAWSPLmqgqLLDNPVLKEIAEKYNKSVAQVIL 212

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19157  213 RWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260

AKR_AKR3D1

cd19121

AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ...

10-279

1.28e-81

AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.

Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 247.83 E-value: 1.28e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIvDGTVKREDIFCTSKVWQ 87
Cdd:cd19121    6 LNTGASIPAVGLGTwqAKAGEV-----KAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPelVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENY--FPKDENGK--FIYDAvDICDTWEAMEKCKDAGLAKSI 163
Cdd:cd19121   80 TYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHdlFPTLPDGSrdLDWDW-NHVDTWKQMEKVLKTGKTKAI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 164 GVCNFNRRQLEKILskPGLKYKPVCNQVECHPYLNQRKLLDFCRV------------DKSFPVLLDDPVLgSMAKKYNRT 231
Cdd:cd19121  157 GVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEkgilieaysplgSTGSPLISDEPVV-EIAKKHNVG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 232 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFqlTSVDMKVLDGL 279
Cdd:cd19121  234 PGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279

AKR_AKR5A_5G

cd19126

AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...

8-280

6.02e-81

AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.

Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 245.42 E-value: 6.02e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   8 VLLNDGHFIPILGFGTSapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCTSKVWQ 87
Cdd:cd19126    1 VTLNNGTRMPWLGLGVF--QTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdenGKFIydavdicDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19126   75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGK-------------DKFI-------DTWKALEKLYASGKVKAIGVSN 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19126  135 FQEHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCK-SKGIVVeawsplgqggLLSNPVLAAIGEKYGKSAAQVVL 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19126  212 RWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254

AKR_AKR2B1-10

cd19113

AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ...

6-285

3.58e-80

AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.

Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 245.43 E-value: 3.58e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19113    1 PDIKLNSGYKMPSVGFGC---WKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKP---GENYFPKDENG---KFIYDAVDICDTWEAMEKCKDAGL 159
Cdd:cd19113   78 WNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFvpiEEKYPPGFYCGdgdNFVYEDVPILDTWKALEKLVDAGK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 160 AKSIGVCNFNRRQLEKILSkpGLKYKPVCNQVECHPYLNQRKLLDFCRVD------------KSF-----------PVLL 216
Cdd:cd19113  158 IKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAgititayssfgpQSFvelnqgralntPTLF 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568981353 217 DDPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19113  236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304

AKR_AKR2A1-2

cd19112

AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ...

7-285

5.00e-80

AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.

Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 245.09 E-value: 5.00e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGT--SAPQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSK 84
Cdd:cd19112    2 TITLNSGHKMPVIGLGVwrMEPGEI-----KELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  85 VWQTFHrpELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKP---GENYFPKDENGKFIYDA-VDICDTWEAMEKCKDAGLA 160
Cdd:cd19112   77 LWNSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDVtISLETTWHAMEKLVSAGLV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV--------------LLDDPVL 221
Cdd:cd19112  155 RSIGISNYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQkhgisVTAHTPLggaaanaewfgsvsPLDDPVL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981353 222 GSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19112  233 KDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296

AKR_AKR2D1

cd19115

AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ...

6-285

3.51e-79

AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.

Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 242.71 E-value: 3.51e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKV 85
Cdd:cd19115    3 PTVKLNSGYDMPLVGFGL---WKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMK---PGENYFP--KDENGKFIYDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19115   80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRVDK------------SF-----------PVLLD 217
Cdd:cd19115  160 RSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGiavtayssfgpqSFleldlpgakdtPPLFE 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568981353 218 DPVLGSMAKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19115  238 HDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305

AKR_GlAR-like

cd19128

Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ...

17-279

1.56e-77

Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.

Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 237.42 E-value: 1.56e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGTsapQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRPELVQ 96
Cdd:cd19128    2 PRLGFGT---YKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  97 VCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPKDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI 176
Cdd:cd19128   79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 177 LSKpgLKYKPVCNQVECHPYLNQRKLLDFC---------------RVDKSFPVLLDDPVLGSMAKKYNRTPALIALRYQV 241
Cdd:cd19128  159 LNY--CKIKPFMNQIECHPYFQNDKLIKFCiennihvtayrplggSYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568981353 242 QR---GVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19128  237 QKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277

AKR_DrGR-like

cd19136

Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ...

16-279

2.26e-77

Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).

Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 236.37 E-value: 2.26e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGT---SAPQEVprSKATEAtkiAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19136    1 MPILGLGTfrlRGEEEV--RQAVDA---ALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  93 ELVQVCLEQSLKQLQLDYVDLYLIHFPIA--MKPgenyfpkdengkfiYDAVDIC---DTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19136   76 EKARAACLGSLERLGTDYLDLYLIHWPGVqgLKP--------------SDPRNAElrrESWRALEDLYKEGKLRAIGVSN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRVDKSF-----------PVLLDDPVLGSMAKKYNRTPALIA 236
Cdd:cd19136  142 YTVRHLEELLKYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHlqaysslgsgdLRLLEDPTVLAIAKKYGRTPAQVL 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568981353 237 LRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19136  220 LRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262

AKR_AKR3C2-3

cd19120

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...

13-285

9.20e-77

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.

Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 235.20 E-value: 9.20e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGT-----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVwq 87
Cdd:cd19120    1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKV-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 tFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGenyfpkdengkfiydAVDICDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19120   75 -SPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKPglKYKPVCNQVECHPYLN--QRKLLDFCR----VDKSF----PVLLD-----DPVLGSMAKKYNRTP 232
Cdd:cd19120  139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCRehgiVVSAYsplsPLTRDaggplDPVLEKIAEKYGVTP 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568981353 233 ALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19120  217 AQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269

AKR_AKR5D1_E1

cd19132

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...

10-280

2.99e-76

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).

Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 233.32 E-value: 2.99e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGTSApqeVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCTSKVWQTF 89
Cdd:cd19132    1 LNDGTQIPAIGFGTYP---LKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 HRPELVQVCLEQSLKQLQLDYVDLYLIHFPIamkpgenyfPKdeNGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFN 169
Cdd:cd19132   74 HGYEEALRTIEESLYRLGLDYVDLYLIHWPN---------PS--RDLYV-------EAWQALIEAREEGLVRSIGVSNFL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 170 RRQLEKILSKPGLKykPVCNQVECHPYLNQRKLLDFCR----VDKSF-PV-----LLDDPVLGSMAKKYNRTPALIALRY 239
Cdd:cd19132  136 PEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHRehgiVTQSWsPLgrgsgLLDEPVIKAIAEKHGKTPAQVVLRW 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568981353 240 QVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19132  214 HVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254

AKR_AKR5A1_2

cd19156

AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ...

8-285

9.20e-76

AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.

Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 232.79 E-value: 9.20e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   8 VLLNDGHFIPILGFGTSAPQEvpRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVWQ 87
Cdd:cd19156    1 VKLANGVEMPRLGLGVWRVQD--GAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdenGKFIydavdicDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19156   75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVK-------------GKFK-------DTWKAFEKLYKEKKVRAIGVSN 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 FNRRQLEKILSKpgLKYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19156  135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCK-EKNIAVeawsplgqgkLLSNPVLKAIGKKYGKSAAQVII 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19156  212 RWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259

AKR_AKR5F1

cd19133

the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...

8-280

2.94e-75

the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).

Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 230.92 E-value: 2.94e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   8 VLLNDGHFIPILGFGTSapqEVPRSKATE-ATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW 86
Cdd:cd19133    1 VTLNNGVEMPILGFGVF---QIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAIK----KSGIPREELFITTKLW 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydavDICDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19133   74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG---------------------DVYGAWRAMEELYKEGKIRAIGVS 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILskPGLKYKPVCNQVECHPYLNQRKLLDFcrvDKSFPV--------------LLDDPVLGSMAKKYNRTP 232
Cdd:cd19133  133 NFYPDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEF---LKKYGVqieawgpfaegrnnLFENPVLTEIAEKYGKSV 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 233 ALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19133  208 AQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255

AKR_AKR3C1

cd19119

Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ...

10-286

2.77e-74

Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).

Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 229.69 E-value: 2.77e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGTSAPQEvPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTF 89
Cdd:cd19119    6 LNTGASIPALGLGTASPHE-DRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 HRPelVQVCLEQSLKQLQLDYVDLYLIHFPIAMK-----PGENYFPKDENGKFIYDA-VDICDTWEAMEKCKDAGLAKSI 163
Cdd:cd19119   85 YDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAAsGDHITTYKQLEKIYLDGRAKAI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 164 GVCNFNRRQLEKILSKpgLKYKPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV------LLDDPVLGSMAKKYNRTP 232
Cdd:cd19119  163 GVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFkhgilVTAYSPLgshgapNLKNPLVKKIAEKYNVST 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353 233 ALIALRYQVQRGVVVLAKSFIEKRIKENMQVfeFQLTSVDMKVLD--GLNKNIRYI 286
Cdd:cd19119  241 GDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDdiGEKYPVRFI 294

AKR_AKR3F3

cd19140

Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...

13-279

9.99e-74

Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.

Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 226.76 E-value: 9.99e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGTSapQEVPRsKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19140    5 GVRIPALGLGTY--PLTGE-ECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIA----ASGVPRDELFLTTKVWPDNYSP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  93 ELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfPKDengkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQ 172
Cdd:cd19140   78 DDFLASVEESLRKLRTDYVDLLLLHWP----------NKD---------VPLAETLGALNEAQEAGLARHIGVSNFTVAL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 173 LEKI--LSKPGLkykpVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQV 241
Cdd:cd19140  139 LREAveLSEAPL----FTNQVEYHPYLDQRKLLDAARehgiaLTAYSPLargeVLKDPVLQEIGRKHGKTPAQVALRWLL 214

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568981353 242 QR-GVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19140  215 QQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253

AKR_AKR2C1

cd19114

AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ...

13-285

2.42e-69

AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.

Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 217.43 E-value: 2.42e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDGTVKREDIFCTSKVWQTFHRP 92
Cdd:cd19114    1 GDKMPLVGFGTA---KIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  93 ELVQVCLEQSLKQLQLDYVDLYLIHFPIAMK---PGENYFP---KDENGKFIYDAVDICDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19114   78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFlwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLD----------------------FCRVDKSFPVLLDDPVLGSM 224
Cdd:cd19114  158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDwakkqgiqitayssfgnavytkVTKHLKHFTNLLEHPVVKKL 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 225 AKKYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19114  236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296

AKR_CeZK1290-like

cd19135

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...

7-279

2.94e-67

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.

Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 210.64 E-value: 2.94e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGTSapqevpRS--KATEATKIAI-DAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTS 83
Cdd:cd19135    4 TVRLSNGVEMPILGLGTS------HSggYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIK----ESGVPREDLFLTT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  84 KVWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENyfPKDEngkfiydavdICDTWEAMEKCKDAGLAKSI 163
Cdd:cd19135   74 KLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN--VKET----------RAETWRALEELYDEGLCRAI 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 164 GVCNFNRRQLEKILSKPGLKykPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPA 233
Cdd:cd19135  142 GVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCR-DNNIVFegycplakgkALEEPTVTELAKKYQKTPA 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568981353 234 LIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19135  219 QILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264

AKR_AKR5H1

cd19134

AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ...

7-285

1.00e-66

AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.

Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 209.33 E-value: 1.00e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   7 TVLLNDGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVW 86
Cdd:cd19134    2 TVTLNDDNTMPVIGLGVG---ELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdENGKFIydavdicDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19134   75 TPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGVS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKILSKPGlkYKPVCNQVECHPYLNQRKLLDFCR----VDKSF-PV----LLDDPVLGSMAKKYNRTPALIAL 237
Cdd:cd19134  137 NFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAqhgiVTQAYsPLgvgrLLDNPAVTAIAAAHGRTPAQVLL 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 238 RYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIRY 285
Cdd:cd19134  215 RWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262

AKR_AKR5B1

cd19127

AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...

10-280

9.98e-64

AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.

Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 201.87 E-value: 9.98e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGTSApqeVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDgtvkREDIFCTSKVWQTF 89
Cdd:cd19127    3 LNNGVEMPALGLGVFQ---TPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVD----RSDIFVTTKLWISD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 HRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMkpgenyfpkdengkfiyDAVDICDTWEAMEKCKDAGLAKSIGVCNFN 169
Cdd:cd19127   76 YGYDKALRGFDASLRRLGLDYVDLYLLHWPVPN-----------------DFDRTIQAYKALEKLLAEGRVRAIGVSNFT 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 170 RRQLEKILSKPGLkyKPVCNQVECHPYLNQRKLLDF-----------------CRVDKSFPV----LLDDPVLGSMAKKY 228
Cdd:cd19127  139 PEHLERLIDATTV--VPAVNQVELHPYFSQKDLRAFhrrlgivtqawspiggvMRYGASGPTgpgdVLQDPTITGLAEKY 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568981353 229 NRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19127  217 GKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268

dkgA

PRK11565

2,5-didehydrogluconate reductase DkgA;

5-268

4.25e-62

2,5-didehydrogluconate reductase DkgA;

Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 197.99 E-value: 4.25e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVL-LNDGHFIPILGFGT-SAPQEVPRSKATEAtkiaIDAGFRHIDCAAVYQNEKEVGLAIRSkivdGTVKREDIFCT 82
Cdd:PRK11565   3 NPTVIkLQDGNVMPQLGLGVwQASNEEVITAIHKA----LEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  83 SKVWQTFHRPelVQVCLEQSLKQLQLDYVDLYLIHFPIAMKpgENYFpkdengkfiydavdicDTWEAMEKCKDAGLAKS 162
Cdd:PRK11565  75 TKLWNDDHKR--PREALEESLKKLQLDYVDLYLMHWPVPAI--DHYV----------------EAWKGMIELQKEGLIKS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 163 IGVCNFNRRQLEKILSKPGLkyKPVCNQVECHPYLNQRKLLDFCRVDK----SFPVL-------LDDPVLGSMAKKYNRT 231
Cdd:PRK11565 135 IGVCNFQIHHLQRLIDETGV--TPVINQIELHPLMQQRQLHAWNATHKiqteSWSPLaqggkgvFDQKVIRDLADKYGKT 212

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568981353 232 PALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEFQL 268
Cdd:PRK11565 213 PAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRL 249

AKR_AKR5C1

cd19130

Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ...

10-280

8.49e-62

Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.

Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 196.67 E-value: 8.49e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGTSapqEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKivdgTVKREDIFCTSKVWQTF 89
Cdd:cd19130    4 LNDGNSIPQLGYGVF---KVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS----GIPRDELFVTTKLWNDR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 HRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKpgenyfpkdenGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFN 169
Cdd:cd19130   77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA-----------GNYV-------HTWEAMIELRAAGRTRSIGVSNFL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 170 RRQLEKILSKPGLKykPVCNQVECHPYLNQRKLLDFCR-----VDKSFPV----LLDDPVLGSMAKKYNRTPALIALRYQ 240
Cdd:cd19130  139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQahdvkIEAWSPLgqgkLLGDPPVGAIAAAHGKTPAQIVLRWH 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568981353 241 VQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:cd19130  217 LQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256

AKR_AKR3E1

cd19122

AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ...

10-266

9.31e-61

AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.

Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 195.15 E-value: 9.31e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  10 LNDGHFIPILGFGTSApQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRSKIVDG-TVKREDIFCTSKVWQT 88
Cdd:cd19122    3 LNNGVKIPAVGFGTFA-NEGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  89 FHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENYFPK-DENGKFIYDAvDICD----TWEAMEKCKDAGLAKSI 163
Cdd:cd19122   82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILK-DLTEnpepTWRAMEEIYESGKAKAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 164 GVCNFNRRQLEKILSKPglKYKPVCNQVECHPYLNQRKLLDFCRVDKSFPV-----------------LLDDPVLGSMAK 226
Cdd:cd19122  161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEaysplgsqnqvpstgerVSENPTLNEVAE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568981353 227 KYNRTPALIALRYQVQRGVVVLAKSFIEKRIKENMQVFEF 266
Cdd:cd19122  239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIEL 278

AKR_AKR3F2

cd19139

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...

16-279

5.98e-60

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).

Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 191.41 E-value: 5.98e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTS--APQEVprskaTEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVW-QTFHRP 92
Cdd:cd19139    1 IPAFGLGTFrlKDDVV-----IDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWiDNLSKD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  93 ELVQvCLEQSLKQLQLDYVDLYLIHFPIamkpgenyfpkdengkfIYDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQ 172
Cdd:cd19139   72 KLLP-SLEESLEKLRTDYVDLTLIHWPS-----------------PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIAL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 173 LEKILSKPGlKYKPVCNQVECHPYLNQRKLLDFCRvDKSFPV----------LLDDPVLGSMAKKYNRTPALIALRYQVQ 242
Cdd:cd19139  134 LDEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCK-QHGIHVtsymtlaygkVLDDPVLAAIAERHGATPAQIALAWAMA 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568981353 243 RGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGL 279
Cdd:cd19139  212 RGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248

AKR_AKR3F1-like

cd19072

Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...

16-277

5.25e-56

Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.

Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 182.04 E-value: 5.25e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSA---PQEVP---RSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRskivdgTVKREDIFCTSKVW 86
Cdd:cd19072    4 VPVLGLGTWGiggGMSKDysdDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITTKVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 QT-FHRPELVQVClEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkdengkfiYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19072   78 PDhLKYDDVIKAA-KESLKRLGTDYIDLYLIHWP-------------------NPSIPIEETLRAMEELVEEGKIRYIGV 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 166 CNFNRRQLEKILSKPGlKYKPVCNQVECHpYLNQR---KLLDFCRvDKSFPVL----LD---------DPVLGSMAKKYN 229
Cdd:cd19072  138 SNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQ-KNGIAIIayspLEkgklsnakgSPLLDEIAKKYG 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568981353 230 RTPALIALRYQVQR-GVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19072  215 KTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263

Aldo_ket_red

pfam00248

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...

19-280

6.38e-54

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.

Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 177.50 E-value: 6.38e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   19 LGFGTSA----PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgTVKREDIFCTSKV------ 85
Cdd:pfam00248   1 IGLGTWQlgggWGPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAmkpgenyfpkdengkfiydAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248  77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIGV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  166 CNFNRRQLEKILSKPglKYKPVCNQVECHPY--LNQRKLLDFCRvDKSFPV----------------------------- 214
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCK-KNGIPLiaysplggglltgkytrdpdkgpgerrrl 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353  215 --------LLDDPVLGSMAKKYNRTPALIALRY--QVQRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLN 280
Cdd:pfam00248 215 lkkgtplnLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290

dkgB

PRK11172

2,5-didehydrogluconate reductase DkgB;

16-284

2.48e-46

2,5-didehydrogluconate reductase DkgB;

Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 157.11 E-value: 2.48e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSAPQEVPrskATEATKIAIDAGFRHIDCAAVYQNEKEVGLAIRskivDGTVKREDIFCTSKVWQTFHRPELV 95
Cdd:PRK11172   3 IPAFGLGTFRLKDQV---VIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKDKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  96 QVCLEQSLKQLQLDYVDLYLIHFPiamKPGenyfpkdengkfiyDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEK 175
Cdd:PRK11172  76 IPSLKESLQKLRTDYVDLTLIHWP---SPN--------------DEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 176 ILSKPGlKYKPVCNQVECHPYLNQRKLLDFCRVD----KSFPVL-----LDDPVLGSMAKKYNRTPALIALRYQVQRGVV 246
Cdd:PRK11172 139 AIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHgihvTSYMTLaygkvLKDPVIARIAAKHNATPAQVILAWAMQLGYS 217

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568981353 247 VLAKSFIEKRIKENMQVFEFQLTSVDMKVLDGLNKNIR 284
Cdd:PRK11172 218 VIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255

AKR_YeaE

cd19138

Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...

6-277

2.09e-43

Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.

Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 149.32 E-value: 2.09e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   6 QTVLLNDGHFIPILGFGTSAPQEVPRSKATE--ATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIF 80
Cdd:cd19138    1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEieALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  81 CTSKVWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkdengkfiyDAVDICDTWEAMEKCKDAGLA 160
Cdd:cd19138   74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR--------------------GGVPLAETVAAMEELKKEGKI 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEKILSKPGLKyKPVCNQVECHpyLNQR----KLLDFCRvDKSFPV---------------LLDDPVL 221
Cdd:cd19138  134 RAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCR-EHGVPVmaysplaqggllrrgLLENPTL 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568981353 222 GSMAKKYNRTPALIALRYQV-QRGVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19138  210 KEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266

AKR_AKR3F1

cd19137

Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...

13-277

3.35e-38

Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.

Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 135.78 E-value: 3.35e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGT------SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSkivdgtVKREDIFCTS 83
Cdd:cd19137    1 GEKIPALGLGTwgiggfLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  84 KVWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgENYFPKDEngkfiydavdicdTWEAMEKCKDAGLAKSI 163
Cdd:cd19137   75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP------NPNIPLEE-------------TLSAMAEGVRQGLIRYI 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 164 GVCNFNRRQLEKILSKpgLKYKPVCNQVECHPY---LNQRKLLDFCR-----VDKSFP----VLLDDPVLGSMAKKYNRT 231
Cdd:cd19137  136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQkngitVVAYSPlrrgLEKTNRTLEEIAKNYGKT 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568981353 232 PALIALRYQVQR-GVVVLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19137  214 IAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260

AKR_AtPLR-like

cd19093

Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...

34-277

1.04e-32

Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.

Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 121.95 E-value: 1.04e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  34 ATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdGTVKREDIFCTSKVWQTFHR--PELVQVCLEQSLKQLQL 108
Cdd:cd19093   28 LQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIATKFAPLPWRltRRSVVKALKASLERLGL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 109 DYVDLYLIHFPiamkpGENYFPkdengkfiydavdICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI---LSKPGlkYK 185
Cdd:cd19093  103 DSIDLYQLHWP-----GPWYSQ-------------IEALMDGLADAVEEGLVRAVGVSNYSADQLRRAhkaLKERG--VP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 186 PVCNQVE---CHPYLNQRKLLDFC-------------------------------RVDKSFPVLLD--DPV---LGSMAK 226
Cdd:cd19093  163 LASNQVEyslLYRDPEQNGLLPACdelgitliaysplaqglltgkyspenpppggRRRLFGRKNLEkvQPLldaLEEIAE 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568981353 227 KYNRTPALIALRYQVQRGVVVL--AKSfiEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19093  243 KYGKTPAQVALNWLIAKGVVPIpgAKN--AEQAEENAGALGWRLSEEEVAELD 293

AKR_AKR11B1-like

cd19084

AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...

13-277

6.24e-32

AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.

Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 119.94 E-value: 6.24e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGTSA-----PQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSK 84
Cdd:cd19084    1 DLKVSRIGLGTWAiggtwWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  85 V---WQTFH------RPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWEAMEKCK 155
Cdd:cd19084   74 CglrWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 156 DAGLAKSIGVCNFNRRQLEKIlskpgLKY-KPVCNQVechPY--LNQ---RKLLDFCR---------------------- 207
Cdd:cd19084  135 KEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRengigvlpygplaqglltgkyk 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 208 VDKSFP--------VLLDDP----------VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVFE 265
Cdd:cd19084  207 KEPTFPpddrrsrfPFFRGEnfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQpgvtSAIVGAKN--PEQLEENAGALD 284

                        330
                 ....*....|..
gi 568981353 266 FQLTSVDMKVLD 277
Cdd:cd19084  285 WELTEEELKEID 296

PdxI

COG0667

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...

5-277

2.87e-30

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];

Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 116.05 E-value: 2.87e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVLLNDGHFIPILGFGT----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvKRE 77
Cdd:COG0667    2 EYRRLGRSGLKVSRLGLGTmtfgGPWGGVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  78 DIFCTSKV--------WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWE 149
Cdd:COG0667   76 DVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------DPD-------TPIEETLG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 150 AMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGLKYKPVCNQVEchpY--LNQR---KLLDFC------------------ 206
Cdd:COG0667  137 ALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRSaeeELLPAArelgvgvlaysplaggll 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 207 --------------RVDKSFPVLLDDP-------VLGSMAKKYNRTPALIALRYQVQRGVVVL----AKSfiEKRIKENM 261
Cdd:COG0667  214 tgkyrrgatfpegdRAATNFVQGYLTErnlalvdALRAIAAEHGVTPAQLALAWLLAQPGVTSvipgARS--PEQLEENL 291

                        330
                 ....*....|....*.
gi 568981353 262 QVFEFQLTSVDMKVLD 277
Cdd:COG0667  292 AAADLELSAEDLAALD 307

AKR_AKR11B3

cd19085

Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...

16-283

2.66e-29

Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.

Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 113.07 E-value: 2.66e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSA--------PQEVPRSKATeaTKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSK 84
Cdd:cd19085    1 VSRLGLGCWQfgggywwgDQDDEESIAT--IHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  85 VWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMkpgenyfpkdengkfiydaVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19085   72 VSPDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSD-------------------VPLEETMEALEKLKEEGKIRAIG 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 165 VCNFNRRQLEKILsKPGlkyKPVCNQVechPY-LNQR----KLLDFCR----------------------VDKSFP---- 213
Cdd:cd19085  133 VSNFGPAQLEEAL-DAG---RIDSNQL---PYnLLWRaieyEILPFCRehgigvlaysplaqglltgkfsSAEDFPpgda 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 214 ----VLLDDP-----------VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVFEFQLTSVDMK 274
Cdd:cd19085  206 rtrlFRHFEPgaeeetfealeKLKEIADELGVTMAQLALAWVLQQpgvtSVIVGARN--PEQLEENAAAVDLELSPSVLE 283


                 ....*....
gi 568981353 275 VLDGLNKNI 283
Cdd:cd19085  284 RLDEISDPL 292

AKR_SF

cd06660

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...

19-249

3.91e-27

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.

Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 105.68 E-value: 3.91e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGTSA-PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtVKREDIFCTSKVWQTFHR--- 91
Cdd:cd06660    3 LGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGdps 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  92 -----PELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd06660   78 rsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------------DPS-------TPVEETLEALNELVREGKIRYIGVS 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 167 NFNRRQLEKIL--SKPGLKYKPVCNQVE---CHPYLNQRKLLDFCRvDKSFPVLlddpVLGSMAkkynRTPALIALRYQV 241
Cdd:cd06660  139 NWSAERLAEALayAKAHGLPGFAAVQPQyslLDRSPMEEELLDWAE-ENGLPLL----AYSPLA----RGPAQLALAWLL 209


                 ....*...
gi 568981353 242 QRGVVVLA 249
Cdd:cd06660  210 SQPFVTVP 217

AKR_unchar

cd19100

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

13-165

8.09e-22

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.

Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 91.77 E-value: 8.09e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  13 GHFIPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRSKivdgtvkREDIFCTSKVWQtfHR 91
Cdd:cd19100    8 GLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGA--RD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981353  92 PELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENyfPKDENGkfiydavdicdTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19100   79 YEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQ--VFGPGG-----------ALEALLEAKEEGKIRFIGI 139

AKR_unchar

cd19099

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

19-165

3.19e-21

Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 91.61 E-value: 3.19e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGTS--APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKIVDGTVKREDIFCTSKV-------- 85
Cdd:cd19099    6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyipgdgd 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 --------------------------WQTFHrPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgENYFPKDENGKFiY 139
Cdd:cd19099   86 eplrplkyleeklgrglidvadsaglRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNP------EEQLLELGEEEF-Y 157

                        170       180
                 ....*....|....*....|....*.
gi 568981353 140 DAVDicDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19099  158 DRLE--EAFEALEEAVAEGKIRYYGI 181

AKR_AKR15A-like

cd19090

AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...

17-165

4.07e-19

AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).

Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 84.91 E-value: 4.07e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGTS----APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRskivdgTVKREDIFCTSKV-----W 86
Cdd:cd19090    1 SALGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALA------ELPREPLVLSTKVgrlpeD 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568981353  87 QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPgenyfpkdengkfiYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19090   75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPW--------------VDILAPGGALEALLELKEEGLIKHIGL 139

AKR_unchar

cd19102

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

16-178

9.89e-19

Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 84.26 E-value: 9.89e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSA-----------PQEVPRSKAteATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSkivdgtVKREDIFC 81
Cdd:cd19102    1 LTTIGLGTWAiggggwgggwgPQDDRDSIA--AIRAALDLGINWIDTAAVYglgHSEEVVGRALKG------LRDRPIVA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  82 T--SKVW------QTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGEnyfpkdengkfiydavdicDTWEAMEK 153
Cdd:cd19102   73 TkcGLLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIE-------------------EAWGALAE 133

                        170       180
                 ....*....|....*....|....*
gi 568981353 154 CKDAGLAKSIGVCNFNRRQLEKILS 178
Cdd:cd19102  134 LKEEGKVRAIGVSNFSVDQMKRCQA 158

COG1453

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];

16-164

2.20e-18

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];

Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 84.10 E-value: 2.20e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVY-QNEKEVGLAIRSKivdgtvkREDIFCTSKVWQTFHRPEL 94
Cdd:COG1453   13 VSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLPPWVRDPED 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  95 VQVCLEQSLKQLQLDYVDLYLIHfpiAMKPGENYfpkdengKFIYDAVDIcdtWEAMEKCKDAGLAKSIG 164
Cdd:COG1453   86 MRKDLEESLKRLQTDYIDLYLIH---GLNTEEDL-------EKVLKPGGA---LEALEKAKAEGKIRHIG 142

AKR_PsAKR

cd19091

Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...

11-277

3.39e-18

Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.

Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 83.05 E-value: 3.39e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  11 NDGHFIPILGFGT-------SAPQEVPRSKATEAT---KIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvkRE 77
Cdd:cd19091    8 RSGLKVSELALGTmtfggggGFFGAWGGVDQEEADrlvDIALDAGINFFDTADVYsegESEEILGKALKGR-------RD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  78 DIFCTSKVwqTFH-----------RPELVQVClEQSLKQLQLDYVDLYLIHFPIAMKPGEnyfpkdengkfiydavdicD 146
Cdd:cd19091   81 DVLIATKV--RGRmgegpndvglsRHHIIRAV-EASLKRLGTDYIDLYQLHGFDALTPLE-------------------E 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 147 TWEAMEKCKDAGLAKSIGVCNFNRRQLEKILS---KPGLKyKPVCNQV-----------ECHPYLNQRKL---------- 202
Cdd:cd19091  139 TLRALDDLVRQGKVRYIGVSNFSAWQIMKALGiseRRGLA-RFVALQAyysllgrdlehELMPLALDQGVgllvwsplag 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 203 -----------------------LDFCRVD--KSFPVLlddPVLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfi 253
Cdd:cd19091  218 gllsgkyrrgqpapegsrlrrtgFDFPPVDreRGYDVV---DALREIAKETGATPAQVALAWLLSRptvsSVIIGARN-- 292

                        330       340
                 ....*....|....*....|....
gi 568981353 254 EKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19091  293 EEQLEDNLGAAGLSLTPEEIARLD 316

AKR_unchar

cd19105

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

5-165

5.96e-18

Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 81.48 E-value: 5.96e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVLLNDGHFIPILGFGTSAPQevprSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRskivdgTVKREDIFC 81
Cdd:cd19105    2 PYRTLGKTGLKVSRLGFGGGGLP----RESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  82 TSKVW---QTFHRPELVQVcLEQSLKQLQLDYVDLYLIHFpiAMKPGENYFpkdeNGKFIydavdicdtwEAMEKCKDAG 158
Cdd:cd19105   72 ATKASprlDKKDKAELLKS-VEESLKRLQTDYIDIYQLHG--VDTPEERLL----NEELL----------EALEKLKKEG 134


                 ....*..
gi 568981353 159 LAKSIGV 165
Cdd:cd19105  135 KVRFIGF 141

AKR_BsYcsN_EcYdhF-like

cd19092

Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...

18-249

9.40e-18

Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.

Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 81.45 E-value: 9.40e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  18 ILGFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgTVKREDIFCTSKV--------- 85
Cdd:cd19092   10 VLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKCgirlgddpr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 -WQTFH---RPELVQVCLEQSLKQLQLDYVDLYLIHFPIA-MKPGEnyfpkdengkfiydavdicdTWEAMEKCKDAGLA 160
Cdd:cd19092   86 pGRIKHydtSKEHILASVEGSLKRLGTDYLDLLLLHRPDPlMDPEE--------------------VAEAFDELVKSGKV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 161 KSIGVCNFNRRQLEkiLSKPGLKYKPVCNQVEC---HPYLNQRKLLDFCRVDKSFP----VLLDDPVLGSMAKKYNRTPA 233
Cdd:cd19092  146 RYFGVSNFTPSQIE--LLQSYLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPmawsPLGGGRLFGGFDERFQRLRA 223

                        250
                 ....*....|....*....
gi 568981353 234 L---IALRYQVQRGVVVLA 249
Cdd:cd19092  224 AleeLAEEYGVTIEAIALA 242

AKR_PA4992-like

cd19095

Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ...

17-169

1.10e-17

Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.

Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 80.74 E-value: 1.10e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGTS----APQEVPRSKATEATKIAIDAGFRHIDCAAVYQN-EKEVGLAIRskivdgTVKREDIFCTSKVWQTF-- 89
Cdd:cd19095    1 SVLGLGTSgigrVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALA------GLRRDDLFIATKVGTHGeg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 ------HRPELVQVCLEQSLKQLQLDYVDLYLIHFPIamkpgenyfPKDENGkfiydavdicDTWEAMEKCKDAGLAKSI 163
Cdd:cd19095   75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPS---------DDELTG----------EVLETLEDLKAAGKVRYI 135


                 ....*.
gi 568981353 164 GVCNFN 169
Cdd:cd19095  136 GVSGDG 141

AKR_Fe-S_oxidoreductase

cd19096

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...

17-265

1.10e-17

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.

Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 80.68 E-value: 1.10e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGT-----SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKV-WQ 87
Cdd:cd19096    1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKLpPW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHfpiAMkpgenyfpkdeNGKFIYDAVDICDTWEAMEKCKDAGLAKSIGvcn 167
Cdd:cd19096   75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH---GL-----------NSPEWLEKARKGGLLEFLEKAKKEGLIRHIG--- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 168 F----NRRQLEKILSkpglkykpvCNQVEC----HPYLNQ-----RKLLDFCRvDKSFPVLLDDPVLGSM---------- 224
Cdd:cd19096  138 FsfhdSPELLKEILD---------SYDFDFvqlqYNYLDQenqagRPGIEYAA-KKGMGVIIMEPLKGGGlannppeala 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568981353 225 -AKKYNRTPALIALRYQV-QRGV-VVLAKSFIEKRIKENMQVFE 265
Cdd:cd19096  208 iLCGAPLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251

AKR_AKR13B1

cd19088

AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...

16-269

1.02e-16

AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.

Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 78.03 E-value: 1.02e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGT---SAPQEV----PRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKIVD-------GTVKRED 78
Cdd:cd19088    1 VSRLGYGAmrlTGPGIWgppaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYPDDvviatkgGLVRTGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  79 ifctsKVWQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyFPKdengkfiydaVDICDTWEAMEKCKDAG 158
Cdd:cd19088   81 -----GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI---------DPK----------VPFEEQLGALAELQDEG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 159 LAKSIGVCNFNRRQLEKILSKPGLkykpVCNQVECHPYlNQR--KLLDFCRVD----------KSFPVLLDDPVLGSMAK 226
Cdd:cd19088  137 LIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLA-NRDdeGVLDYCEAAgiafipwfplGGGDLAQPGGLLAEVAA 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568981353 227 KYNRTPALIALRYQVQRGVVVLA---KSFIEkRIKENMQVFEFQLT 269
Cdd:cd19088  212 RLGATPAQVALAWLLARSPVMLPipgTSSVE-HLEENLAAAGLRLS 256

AKR_AKR11C1

cd19086

AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...

20-166

2.78e-16

AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.

Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 76.36 E-value: 2.78e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  20 GFGTSAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSKV---------WQ 87
Cdd:cd19086   12 GLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFgnrfdggpeRP 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568981353  88 TFHRPELVQVCLEQSLKQLQLDYVDLYLIHfpiamKPGENYFPKDEngkfiydavdicdTWEAMEKCKDAGLAKSIGVC 166
Cdd:cd19086   85 QDFSPEYIREAVEASLKRLGTDYIDLYQLH-----NPPDEVLDNDE-------------LFEALEKLKQEGKIRAYGVS 145

AKR_AKR11B2

cd19149

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...

16-175

3.13e-16

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.

Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 77.31 E-value: 3.13e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGT------SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSK-- 84
Cdd:cd19149   11 ASVIGLGTwaigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLATKcg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  85 -VW---QTFH-------------RPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgENYFPkdengkfiydavdICDT 147
Cdd:cd19149   84 lRWdreGGSFffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQ------DVETP-------------IEET 144

                        170       180
                 ....*....|....*....|....*...
gi 568981353 148 WEAMEKCKDAGLAKSIGVCNFNRRQLEK 175
Cdd:cd19149  145 MEALEELKRQGKIRAIGASNVSVEQIKE 172

AKR_AKR11A1_11D1

cd19083

AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...

39-174

3.66e-16

AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).

Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 77.07 E-value: 3.66e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  39 KIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvKREDIFCTSKVWQTF--------HRPELVQVCLEQSLKQLQ 107
Cdd:cd19083   40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFggdgsvlnNSPEFLRSAVEKSLKRLN 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568981353 108 LDYVDLYLIHFPiamkpgENYFPKDEngkfiydAVDicdtweAMEKCKDAGLAKSIGVCNFNRRQLE 174
Cdd:cd19083  114 TDYIDLYYIHFP------DGETPKAE-------AVG------ALQELKDEGKIRAIGVSNFSLEQLK 161

AKR_AKR11B1

cd19148

Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...

33-174

3.81e-14

Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.

Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 71.18 E-value: 3.81e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  33 KATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdGTVKREDIFCTSKV---W---QTFHR---PELVQVCLE 100
Cdd:cd19148   26 EAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVgleWdegGEVVRnssPARIRKEVE 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981353 101 QSLKQLQLDYVDLYLIHFPiamkpgenyfpkDEngkfiydAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLE 174
Cdd:cd19148  101 DSLRRLQTDYIDLYQVHWP------------DP-------LVPIEETAEALKELLDEGKIRAIGVSNFSPEQME 155

Aldo_ket_red_shaker-like

cd19074

Shaker potassium channel beta subunit family and similar proteins; This family includes ...

19-207

9.52e-14

Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.

Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 70.31 E-value: 9.52e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGT--SAPQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKV-WQT---- 88
Cdd:cd19074    7 LSLGTwlTFGGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKALK------GWPRESYVISTKVfWPTgpgp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  89 ----FHRPELVQvCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19074   81 ndrgLSRKHIFE-SIHASLKRLQLDYVDIYYCHRY------------DPE-------TPLEETVRAMDDLIRQGKILYWG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568981353 165 VCNFNRRQLEKI--LSKPGLKYKPVCNQVECHpYLNQRK---LLDFCR 207
Cdd:cd19074  141 TSEWSAEQIAEAhdLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCE 187

AKR_FDH

cd19162

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...

17-165

9.29e-13

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.

Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 67.38 E-value: 9.29e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGTSAPQEVPRSKATEATKI---AIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvKREDIFCTSKV----- 85
Cdd:cd19162    1 PRLGLGAASLGNLARAGEDEAAATldaAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrlle 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 -----WQTFHRPEL------VQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDEngkfiYDAVDICDTWEAMEKC 154
Cdd:cd19162   75 pgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DR-----HLLQALTDAFPALEEL 137

                        170
                 ....*....|.
gi 568981353 155 KDAGLAKSIGV 165
Cdd:cd19162  138 RAEGVVGAIGV 148

AKR_unchar

cd19101

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

31-277

2.35e-12

Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 66.08 E-value: 2.35e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  31 RSKATEATKIAIDAGFRHIDCAAVYQNEKE-VGLAIRSKIVDGTVKREDIFCTSkvWQTFHR-----PELVQVCLEQSLK 104
Cdd:cd19101   22 EDAAVRAMAAYVDAGLTTFDCADIYGPAEElIGEFRKRLRRERDAADDVQIHTK--WVPDPGeltmtRAYVEAAIDRSLK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 105 QLQLDYVDLYLIHFpiamkpgENYfpkdENGKFIydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPglkY 184
Cdd:cd19101  100 RLGVDRLDLVQFHW-------WDY----SDPGYL-------DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---V 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 185 KPVCNQVEcHPYLNQR---KLLDFCR-----------------------VDKSFPVLLDDP------------------- 219
Cdd:cd19101  159 PIVSNQVQ-YSLLDRRpenGMAALCEdhgikllaygtlaggllsekylgVPEPTGPALETRslqkyklmidewggwdlfq 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568981353 220 ----VLGSMAKKYNRTPALIALRYQVQR----GVVVLAKSfiEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19101  238 ellrTLKAIADKHGVSIANVAVRWVLDQpgvaGVIVGARN--SEHIDDNVRAFSFRLDDEDRAAID 301

AKR_AKR9C1

cd19081

AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...

42-277

6.57e-12

AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).

Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 64.93 E-value: 6.57e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  42 IDAGFRHIDCAAVYQNEKEVGLAIRSKIVDG-----TVKREDIFCTSKV--WQTFHRPEL----VQVCLEQSLKQLQLDY 110
Cdd:cd19081   36 VDAGGNFIDTADVYSAWVPGNAGGESETIIGrwlksRGKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRRLQTDY 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 111 VDLYLIHFPiamkpgenyfpkDengkfiyDAVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL--SKPGLKYKPVC 188
Cdd:cd19081  116 IDLYQAHWD------------D-------PATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALelSRQHGLPRYVS 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 189 NQVEchpY-LNQRK-----LLDFCR--------------------------VDKSFPV------LLDDP------VLGSM 224
Cdd:cd19081  177 LQPE---YnLVDREsfegeLLPLCReegigvipysplaggfltgkyrseadLPGSTRRgeaakrYLNERglrildALDEV 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568981353 225 AKKYNRTPALIALRYQVQRGVV--VLAKSFIEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19081  254 AAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308

AKR_EcYajO-like

cd19079

Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...

36-277

1.10e-11

Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.

Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 64.14 E-value: 1.10e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  36 EATKI---AIDAGFRHIDCAAVYQN---EKEVGLAIRSKIvdgtvKREDIFCTSKVW-QTFHRPE---------LVQVcl 99
Cdd:cd19079   36 ESRPIikrALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYfPMGDGPNgrglsrkhiMAEV-- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 100 EQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKIL-- 177
Cdd:cd19079  109 DASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALhl 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 178 -SKPGLKyKPVCNQvechPYLN------QRKLLDFCR-----------------------VDKSFPVLLDDPVLGS---- 223
Cdd:cd19079  170 aEKNGWT-KFVSMQ----NHYNllyreeEREMIPLCEeegigvipwsplargrlarpwgdTTERRRSTTDTAKLKYdyft 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 224 ------------MAKKYNRTPALIALRYQVQRGVVV-----LAKsfiEKRIKENMQVFEFQLTSVDMKVLD 277
Cdd:cd19079  245 eadkeivdrveeVAKERGVSMAQVALAWLLSKPGVTapivgATK---LEHLEDAVAALDIKLSEEEIKYLE 312

AKR_AKR13A1

cd19144

AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...

5-288

1.14e-11

AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.

Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 64.39 E-value: 1.14e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353   5 QQTVLLNDGHFIPILGFGT---SAPQEvPRSKATEATKI---AIDAGFRHIDCAAVYQ-NEKEVGLAIRSKivdgTVKRE 77
Cdd:cd19144    2 PTRTLGRNGPSVPALGFGAmglSAFYG-PPKPDEERFAVldaAFELGCTFWDTADIYGdSEELIGRWFKQN----PGKRE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  78 DIFCTSKVWQTFHR----------PELVQVCLEQSLKQLQLDYVDLYLIHFPIAMKPGENyfpkdengkfiydavdicdT 147
Cdd:cd19144   77 KIFLATKFGIEKNVetgeysvdgsPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEK-------------------T 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 148 WEAMEKCKDAGLAKSIGV--CNFNR-RQLEKI--LSKPGLKYKPVCNQVEchpyLNQRKLLDFCR--------------- 207
Cdd:cd19144  138 VAAMAELVQEGKIKHIGLseCSAETlRRAHAVhpIAAVQIEYSPFSLDIE----RPEIGVLDTCRelgvaivaysplgrg 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 208 ------------------------VDKSFPV---LLDDpvLGSMAKKYNRTPALIALRYQVQRG--VVVLAKSFIEKRIK 258
Cdd:cd19144  214 fltgairspddfeegdfrrmaprfQAENFPKnleLVDK--IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLE 291

                        330       340       350
                 ....*....|....*....|....*....|
gi 568981353 259 ENMQVFEFQLTSVDMKVLDGLNKNIRYIGS 288
Cdd:cd19144  292 ENLGALKVKLTEEEEKEIREIAEEAEVVGE 321

AKR_AKR12A1_B1_C1

cd19087

AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...

30-177

3.77e-11

AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.

Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 62.59 E-value: 3.77e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  30 PRSKATEATKI---AIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSKVWQTFH---------RPEL 94
Cdd:cd19087   25 GRTDEETSFAImdrALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFGPMGddpndrglsRRHI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  95 VQVClEQSLKQLQLDYVDLYLIHFPIAMKPGEnyfpkdengkfiydavdicDTWEAMEKCKDAGLAKSIGVCNFNRRQLE 174
Cdd:cd19087   98 RRAV-EASLRRLQTDYIDLYQMHHFDRDTPLE-------------------ETLRALDDLVRQGKIRYIGVSNFAAWQIA 157


                 ...
gi 568981353 175 KIL 177
Cdd:cd19087  158 KAQ 160

AKR_AKR13A_13D

cd19076

AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...

41-164

4.64e-11

AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.

Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 62.23 E-value: 4.64e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  41 AIDAGFRHIDCAAVYQ---NEKEVGLAIRSKivdgtvkREDIFCTSK---VWQTFH-------RPELVQVCLEQSLKQLQ 107
Cdd:cd19076   41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATKfgiVRDPGSgfrgvdgRPEYVRAACEASLKRLG 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568981353 108 LDYVDLYLIHFPiamkpgenyfpkDENgkfiydaVDICDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19076  114 TDVIDLYYQHRV------------DPN-------VPIEETVGAMAELVEEGKVRYIG 151

AKR_AKR7A1-5

cd19075

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...

18-207

5.25e-11

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.

Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 62.19 E-value: 5.25e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  18 ILG---FGTSAPQEVPrSKATEATKIAIDAGFRHIDCAAVYQN---EK---EVGLAIRSKIVDgtvkredifctSKV--- 85
Cdd:cd19075    4 ILGtmtFGSQGRFTTA-EAAAELLDAFLERGHTEIDTARVYPDgtsEEllgELGLGERGFKID-----------TKAnpg 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 WQTFHRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgenyfpkDEngkfiydAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19075   72 VGGGLSPENVRKQLETSLKRLKVDKVDVFYLHAP------------DR-------STPLEETLAAIDELYKEGKFKEFGL 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568981353 166 CNFNRRQLEKILS--------KP----GLkYKPVCNQVEchpylnqRKLLDFCR 207
Cdd:cd19075  133 SNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLR 178

AKR_Tas-like

cd19094

Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...

36-167

9.08e-11

Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.

Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 61.81 E-value: 9.08e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  36 EATKI---AIDAGFRHIDCAAVY---QNEKEVGLA--IRSKIVDGTVKREDIFCTSKV-----WQTFHR-------PELV 95
Cdd:cd19094   19 EAHEQldyAFDEGVNFIDTAEMYpvpPSPETQGRTeeIIGSWLKKKGNRDKVVLATKVagpgeGITWPRgggtrldRENI 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568981353  96 QVCLEQSLKQLQLDYVDLYLIHFP---IAMKPGENYFPKDENgkfiYDAVDICDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:cd19094   99 REAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEE----EDSVSFEEQLEALGELVKAGKIRHIGLSN 169

AKR_unchar

cd19104

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

31-164

1.85e-10

Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 60.74 E-value: 1.85e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  31 RSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvkREDIFCTSKV-WQTFHRPELVQV---CLEQSL 103
Cdd:cd19104   31 REEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVrLDPDDLGDIGGQierSVEKSL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 104 KQLQLDYVDLYLIHFPIAMKPGEnyfPKDENGKFIYDAVDIcDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19104  104 KRLKRDSVDLLQLHNRIGDERDK---PVGGTLSTTDVLGLG-GVADAFERLRSEGKIRFIG 160

AKR_galDH

cd19163

L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...

16-205

3.33e-10

L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).

Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 59.87 E-value: 3.33e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSA----PQEVPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKV--- 85
Cdd:cd19163   13 VSKLGFGASPlggvFGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATKVgry 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  86 ----WQTF-HRPELVQVCLEQSLKQLQLDYVDLYLIHFPiamkpgEnyFPKDENgkfiydaVDICDTWEAMEKCKDAGLA 160
Cdd:cd19163   87 gldpDKMFdFSAERITKSVEESLKRLGLDYIDIIQVHDI------E--FAPSLD-------QILNETLPALQKLKEEGKV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568981353 161 KSIGVCNFNRRQLEKILSKPG------LKYkpvcnqveCHPYLNQRKLLDF 205
Cdd:cd19163  152 RFIGITGYPLDVLKEVLERSPvkidtvLSY--------CHYTLNDTSLLEL 194

AKR_AKR15A

cd19152

AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...

17-165

1.08e-09

AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.

Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 58.39 E-value: 1.08e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  17 PILGFGTSAP----QEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvKREDIFCTSKVWQTF 89
Cdd:cd19152    1 PKLGFGTAPLgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVGRLL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  90 -------------------HRPEL------VQVCLEQSLKQLQLDYVDLYLIHFPiamkpgENYFPKDENGKFIYDAVDi 144
Cdd:cd19152   75 vplqeveptfepgfwnplpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDEHFAQAIK- 147

                        170       180
                 ....*....|....*....|.
gi 568981353 145 cDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19152  148 -GAFRALEELREEGVIKAIGL 167

tas

PRK10625

putative aldo-keto reductase; Provisional

14-167

2.49e-08

putative aldo-keto reductase; Provisional

Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 2.49e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  14 HFIP-------ILGFGT-SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQ----------NEKEVGLAIRSKivdgtVK 75
Cdd:PRK10625   4 HRIPhsslevsTLGLGTmTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  76 REDIFCTSKVW-------------QTFHRPElVQVCLEQSLKQLQLDYVDLYLIHFPiaMKPgENYFpkdenGKFIYD-- 140
Cdd:PRK10625  79 REKLIIASKVSgpsrnndkgirpnQALDRKN-IREALHDSLKRLQTDYLDLYQVHWP--QRP-TNCF-----GKLGYSwt 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568981353 141 ----AVDICDTWEAMEKCKDAGLAKSIGVCN 167
Cdd:PRK10625 150 dsapAVSLLETLDALAEQQRAGKIRYIGVSN 180

AKR_AKR10A1_2

cd19082

AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...

19-167

3.65e-08

AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.

Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 53.71 E-value: 3.65e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGTS-APQEVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEVGlaiRSKIVDG-----TVKREDIFCTSK----VWQT 88
Cdd:cd19082    3 IVLGTAdFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERG---ASERVIGewlksRGNRDKVVIATKgghpDLED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  89 FHR----PELVQVCLEQSLKQLQLDYVDLYLIH-----FPIamkpgenyfpkdenGKFIydavdicdtwEAMEKCKDAGL 159
Cdd:cd19082   80 MSRsrlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV--------------GEIV----------DTLNELVRAGK 135


                 ....*...
gi 568981353 160 AKSIGVCN 167
Cdd:cd19082  136 IRAFGASN 143

AKR_AKR6B1

cd19142

AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...

16-225

4.33e-08

AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.

Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 53.62 E-value: 4.33e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGT--SAPQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgTVKREDIFCTSKV-WQT- 88
Cdd:cd19142   13 VSNVGLGTwsTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKK----GWKRSSYIVSTKIyWSYg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  89 -----FHRPELVQvCLEQSLKQLQLDYVDLYLIHFPIAMKPGE------NYFPKdeNGKFIYDAvdiCDTWEAMEkckda 157
Cdd:cd19142   89 seergLSRKHIIE-SVRASLRRLQLDYIDIVIIHKADPMCPMEevvramSYLID--NGLIMYWG---TSRWSPVE----- 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 158 gLAKSIGVCnfnrRQLEKILskpglkykPVCNQVECHPylnqrklldFCR--VDKSFPVLLDDPVLGSMA 225
Cdd:cd19142  158 -IMEAFSIA----RQFNCPT--------PICEQSEYHM---------FCRekMELYMPELYNKVGVGLIT 205

AKR_unchar

cd19097

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

35-184

5.03e-08

Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 52.91 E-value: 5.03e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  35 TEATKI---AIDAGFRHIDCAAVYQN-EKEVGLAIRSKivdgtvkrEDIFCTSKV----WQTFHRPELVQVCLEQSLKQL 106
Cdd:cd19097   26 KEAKKIleyALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRL 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568981353 107 QLDYVDLYLIHFPIAMkpgenyfpkDENGKFIydavdicdtWEAMEKCKDAGLAKSIGVCNFNRRQLEKILSKPGLKY 184
Cdd:cd19097   98 KVDSLDGLLLHNPDDL---------LKHGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI 157

AKR_AKR6C1_2

cd19143

AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...

21-119

1.19e-07

AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.

Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 52.21 E-value: 1.19e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  21 FGTsapqEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRskivDGTVKREDIFCTSKV-W---------Q 87
Cdd:cd19143   24 FGN----QVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK----ELGWPRSDYVVSTKIfWggggpppndR 95

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568981353  88 TFHRPELVQVClEQSLKQLQLDYVDLYLIHFP 119
Cdd:cd19143   96 GLSRKHIVEGT-KASLKRLQLDYVDLVFCHRP 126

AKR_unchar

cd19103

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

41-207

2.02e-07

Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 51.57 E-value: 2.02e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  41 AIDAGFRHIDCAAVY---QNEKEVGLAIRskivdgTVKREDIFCTSKvwqtF------HRPELVQVCLEQSLKQLQLDYV 111
Cdd:cd19103   41 AMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTK----FtpqiagQSADPVADMLEGSLARLGTDYI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 112 DLYLIHFPiamkpgenyfpkdengkfiydaVDIcDTW--EAMEKCKDaGLAKSIGVCNFNRRQLEK---ILSKPGLKYKP 186
Cdd:cd19103  111 DIYWIHNP----------------------ADV-ERWtpELIPLLKS-GKVKHVGVSNHNLAEIKRaneILAKAGVSLSA 166

                        170       180
                 ....*....|....*....|....*.
gi 568981353 187 VCNqvecHPYLNQRK-----LLDFCR 207
Cdd:cd19103  167 VQN----HYSLLYRSseeagILDYCK 188

AKR_galDH-like

cd19153

L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...

19-222

4.11e-07

L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).

Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 50.61 E-value: 4.11e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGTSA-----PQEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgTVKREDIFCTSKVWQ--- 87
Cdd:cd19153   15 VGLGTAAlggvyGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGRyrd 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  88 -TF-HRPELVQVCLEQSLKQLQLDYVDLYLIHfpiamkpgenyfpkdeNGKFIYDAVDICDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19153   91 sEFdYSAERVRASVATSLERLHTTYLDVVYLH----------------DIEFVDYDTLVDEALPALRTLKDEGVIKRIGI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 166 CNFNRRQLEKIL--SKPGlkyKPVCNQVECHPYLNQRKLLDFCR--VDKSFPVLLDDPVLG 222
Cdd:cd19153  155 AGYPLDTLTRATrrCSPG---SLDAVLSYCHLTLQDARLESDAPglVRGAGPHVINASPLS 212

AKR_AKR13C1_2

cd19078

AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...

31-117

1.20e-06

AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.

Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 49.15 E-value: 1.20e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  31 RSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKivdgtvkREDIFCTSKVWQTFH-----------RPELVQ 96
Cdd:cd19078   24 KEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFKIDggkpgplgldsRPEHIR 96

                         90       100
                 ....*....|....*....|.
gi 568981353  97 VCLEQSLKQLQLDYVDLYLIH 117
Cdd:cd19078   97 KAVEGSLKRLQTDYIDLYYQH 117

AKR_unchar

cd19752

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...

42-222

1.75e-06

Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 48.48 E-value: 1.75e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  42 IDAGFRHIDCAAVY----------QNEKEVG--LAIRSKivdgtvkREDIFCTSKVWQTFHRP------------ELVQV 97
Cdd:cd19752   27 VAAGGNFLDTANNYafwteggvggESERLIGrwLKDRGN-------RDDVVIATKVGAGPRDPdggpespeglsaETIEQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  98 CLEQSLKQLQLDYVDLYLIHfpiamkpgenyfpkdengkfIYD-AVDICDTWEAMEKCKDAGLAKSIGVCNFNRRQLEKI 176
Cdd:cd19752  100 EIDKSLRRLGTDYIDLYYAH--------------------VDDrDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981353 177 --LSKPGLKYKPVCNQVEcHPYL---------NQR----KLLDFCRVDKSFPVLLDDPVLG 222
Cdd:cd19752  160 rqIARQQGWAEFSAIQQR-HSYLrprpgadfgVQRivtdELLDYASSRPDLTLLAYSPLLS 219

AKR_AKR9A_9B

cd19080

AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...

42-126

2.98e-06

AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.

Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 47.98 E-value: 2.98e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  42 IDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvkREDIFCTSKVwqTF------------HRPELVQvCLEQSLKQL 106
Cdd:cd19080   41 VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKY--TMnrrpgdpnaggnHRKNLRR-SVEASLRRL 110

                         90       100
                 ....*....|....*....|
gi 568981353 107 QLDYVDLYLIHFPIAMKPGE 126
Cdd:cd19080  111 QTDYIDLLYVHAWDFTTPVE 130

AKR_AKR13D1

cd19145

AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...

29-126

8.89e-06

AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.

Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 46.27 E-value: 8.89e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  29 VPRSKATEATKIAIDAGFRHIDCAAVY---QNEKEVGLAIRSKIvdgtvkREDIFCTSKVWQTFHR---------PELVQ 96
Cdd:cd19145   30 KPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------REKVQLATKFGIHEIGgsgvevrgdPAYVR 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568981353  97 VCLEQSLKQLQLDYVDLYLIH-----FPIAMKPGE 126
Cdd:cd19145  104 AACEASLKRLDVDYIDLYYQHridttVPIEITMGE 138

AKR_AKR14A1_2

cd19089

AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...

41-191

1.32e-04

AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.

Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 43.01 E-value: 1.32e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  41 AIDAGFRHIDCAAVY-----QNEKEVGLAIRSkivDGTVKREDIFCTSKV-WQTFHRP--------ELVQvCLEQSLKQL 106
Cdd:cd19089   38 AFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKAgYGMWPGPygdggsrkYLLA-SLDQSLKRM 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353 107 QLDYVDLYLIHfpiamKPGENYfPKDENGKFIYDAVdicdtweamekckDAGLAKSIGVCNFNRRQLEK---ILSKpgLK 183
Cdd:cd19089  114 GLDYVDIFYHH-----RYDPDT-PLEETMTALADAV-------------RSGKALYVGISNYPGAKARRaiaLLRE--LG 172


                 ....*...
gi 568981353 184 YKPVCNQV 191
Cdd:cd19089  173 VPLIIHQP 180

AKR_ARA2

cd19164

D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...

18-117

2.85e-04

D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).

Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 41.88 E-value: 2.85e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  18 ILGFGTSAPQ---EVPRSKATEATKIAIDAGFRHIDCAAVYQNEKEV-GLAIrsKIVDGTVKREDIFCTSKV-----WQT 88
Cdd:cd19164   17 IFGAATFSYQyttDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIIlGRAL--KALRDEFPRDTYFIITKVgrygpDDF 94

                         90       100
                 ....*....|....*....|....*....
gi 568981353  89 FHRPELVQVCLEQSLKQLQLDYVDLYLIH 117
Cdd:cd19164   95 DYSPEWIRASVERSLRRLHTDYLDLVYLH 123

AKR_AKR15A1

cd19161

Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ...

19-164

4.89e-04

Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.

Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 41.16 E-value: 4.89e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  19 LGFGTsAP-----QEVPRSKATEATKIAIDAGFRHIDCAAVYQN---EKEVGLAIRSKivdgtvKREDIFCTSKVW---- 86
Cdd:cd19161    3 LGLGT-AGlgnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREK------PRDEFVLSTKVGrllk 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 --QTFHRP-------ELVQVC------------LEQSLKQLQLDYVDLYLIH----FPIAMKPGENYFPKDENGKFiyda 141
Cdd:cd19161   76 paREGSVPdpngfvdPLPFEIvydysydgimrsFEDSLQRLGLNRIDILYVHdigvYTHGDRKERHHFAQLMSGGF---- 151

                        170       180
                 ....*....|....*....|...
gi 568981353 142 vdicdtwEAMEKCKDAGLAKSIG 164
Cdd:cd19161  152 -------KALEELKKAGVIKAFG 167

Aldo_ket_red_shaker

cd19141

Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...

16-225

3.09e-03

Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.

Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 38.58 E-value: 3.09e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  16 IPILGFGTSAP--QEVPRSKATEATKIAIDAGFRHIDCAAVYQNEK-EV--GLAIRSKivdgTVKREDIFCTSKV-W--- 86
Cdd:cd19141   12 VSCLGLGTWVTfgSQISDEVAEELVTLAYENGINLFDTAEVYAAGKaEIvlGKILKKK----GWRRSSYVITTKIfWggk 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981353  87 ----QTFHRPELVQvCLEQSLKQLQLDYVDLYLIHFPIAMKPGENY---FPKDEN-GKFIYDAVdicDTWEAMEKCKDAG 158
Cdd:cd19141   88 aeteRGLSRKHIIE-GLKASLERLQLEYVDIVFANRPDPNTPMEEIvraFTHVINqGMAMYWGT---SRWSAMEIMEAYS 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568981353 159 LAksigvcnfnrRQLEKIlskpglkyKPVCNQVECHpyLNQRKlldfcRVDKSFPVLLDDPVLGSMA 225
Cdd:cd19141  164 VA----------RQFNLI--------PPIVEQAEYH--LFQRE-----KVEMQLPELFHKIGVGAMT 205

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01