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Conserved domains on  [gi|1720403833|ref|XP_030108451|]
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S-adenosylhomocysteine hydrolase-like protein 1 isoform X2 [Mus musculus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 21-288 0e+00

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member smart00996:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 426  Bit Score: 550.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833   21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:smart00996 158 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT-PELTWERVR 179
Cdd:smart00996 238 IDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIK 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  180 SQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPS 258
Cdd:smart00996 318 PQVDHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEK 396

                          250       260       270
                   ....*....|....*....|....*....|
gi 1720403833  259 FDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:smart00996 397 LGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
21-288 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 550.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833   21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:smart00996 158 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT-PELTWERVR 179
Cdd:smart00996 238 IDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIK 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  180 SQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPS 258
Cdd:smart00996 318 PQVDHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEK 396

                          250       260       270
                   ....*....|....*....|....*....|
gi 1720403833  259 FDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:smart00996 397 LGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
21-288 6.52e-178

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 497.35  E-value: 6.52e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVTSLRTPELTWERV 178
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 179 RsQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 257
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720403833 258 SFDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 21-277 9.67e-169

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 473.10  E-value: 9.67e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:cd00401   146 LRAMEKEGKLLFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTE 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:cd00401   226 VDPICALQAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:cd00401   306 QVDEYTLPDGRRIILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEAL 384

                         250
                  ....*....|....*...
gi 1720403833 260 DAHLTELTDDQAKYLGLN 277
Cdd:cd00401   385 GIKLDKLTEEQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 21-283 3.04e-145

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 414.52  E-value: 3.04e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:PRK05476  163 LYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:PRK05476  243 VDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKP 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:PRK05476  323 QVDEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKAL 401

                         250       260
                  ....*....|....*....|....
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGPFK 283
Cdd:PRK05476  402 GVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
21-281 4.86e-141

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 403.66  E-value: 4.86e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:COG0499   160 LRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:COG0499   240 VDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRP 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCSTV-PTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:COG0499   320 QVDEYTLPDGRRIYLLAEGRLVNLAAATGhPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEAL 398

                         250       260
                  ....*....|....*....|..
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGP 281
Cdd:COG0499   399 GVKIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 21-281 5.47e-110

adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]


Pssm-ID: 213572  Cd Length: 407  Bit Score: 324.36  E-value: 5.47e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:TIGR00936 147 LRAMEAEGVLKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:TIGR00936 227 VDPIRALEAAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRP 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:TIGR00936 307 QVDEYILKDGRRIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAM 385

                         250       260
                  ....*....|....*....|..
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGP 281
Cdd:TIGR00936 386 GIEIDELTEEQKEYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
21-288 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 550.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833   21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:smart00996 158 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT-PELTWERVR 179
Cdd:smart00996 238 IDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIK 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  180 SQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPS 258
Cdd:smart00996 318 PQVDHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEK 396

                          250       260       270
                   ....*....|....*....|....*....|
gi 1720403833  259 FDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:smart00996 397 LGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
21-288 6.52e-178

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 497.35  E-value: 6.52e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVTSLRTPELTWERV 178
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 179 RsQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 257
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720403833 258 SFDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 21-277 9.67e-169

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 473.10  E-value: 9.67e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:cd00401   146 LRAMEKEGKLLFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTE 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:cd00401   226 VDPICALQAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:cd00401   306 QVDEYTLPDGRRIILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEAL 384

                         250
                  ....*....|....*...
gi 1720403833 260 DAHLTELTDDQAKYLGLN 277
Cdd:cd00401   385 GIKLDKLTEEQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 21-283 3.04e-145

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 414.52  E-value: 3.04e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:PRK05476  163 LYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:PRK05476  243 VDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKP 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:PRK05476  323 QVDEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKAL 401

                         250       260
                  ....*....|....*....|....
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGPFK 283
Cdd:PRK05476  402 GVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
21-281 4.86e-141

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 403.66  E-value: 4.86e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:COG0499   160 LRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:COG0499   240 VDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRP 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCSTV-PTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:COG0499   320 QVDEYTLPDGRRIYLLAEGRLVNLAAATGhPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEAL 398

                         250       260
                  ....*....|....*....|..
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGP 281
Cdd:COG0499   399 GVKIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 21-288 4.38e-140

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 403.27  E-value: 4.38e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:PTZ00075  205 LYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT-PELTWERVR 179
Cdd:PTZ00075  285 IDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIK 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 180 SQVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELY-NAPEGRYKQDVYLLPKKMDEYVASLHLP 257
Cdd:PTZ00075  365 PQVDRYTFPDGKGIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWeNRDTGKYPNGVYKLPKELDEKVARLHLK 444

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720403833 258 SFDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:PTZ00075  445 KLGAKLTKLTDKQAEYIGVPVDGPYKSDHYR 475
PLN02494 PLN02494
adenosylhomocysteinase
 21-288 2.12e-117

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 345.69  E-value: 2.12e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:PLN02494  205 LYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT-PELTWERVR 179
Cdd:PLN02494  285 IDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIK 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 180 SQVDHVIWPDGKR-VVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPE-GRYKQDVYLLPKKMDEYVASLHL 256
Cdd:PLN02494  365 PQTDRWVFPDTGSgIIVLAEGRLMNLGCATgHPSFVMSCSFTNQVIAQLELWNEKKsGKYEKKVYVLPKHLDEKVAALHL 444

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720403833 257 PSFDAHLTELTDDQAKYLGLNKNGPFKPNYYR 288
Cdd:PLN02494  445 GKLGAKLTKLSKDQADYINVPVEGPYKPAHYR 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 21-281 5.47e-110

adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]


Pssm-ID: 213572  Cd Length: 407  Bit Score: 324.36  E-value: 5.47e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  21 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITE 100
Cdd:TIGR00936 147 LRAMEAEGVLKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 101 IDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRS 180
Cdd:TIGR00936 227 VDPIRALEAAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRP 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 181 QVDHVIWPDGKRVVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPSF 259
Cdd:TIGR00936 307 QVDEYILKDGRRIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAM 385

                         250       260
                  ....*....|....*....|..
gi 1720403833 260 DAHLTELTDDQAKYLGLNKNGP 281
Cdd:TIGR00936 386 GIEIDELTEEQKEYLGSWEEGT 407
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
48-208 8.56e-108

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 309.67  E-value: 8.56e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  48 NLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLNEVIRQVD 127
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833 128 VVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRSQVDHVIWPDGKRVVLLAEGRLLNLSCS 207
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  .
gi 1720403833 208 T 208
Cdd:pfam00670 161 T 161
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
48-209 2.15e-104

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 300.91  E-value: 2.15e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833   48 NLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLNEVIRQVD 127
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  128 VVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRSQVDHVIWPDGKRVVLLAEGRLLNLSCS 207
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 1720403833  208 TV 209
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 27-228 2.91e-29

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 113.09  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  27 AGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGG----------KQVVVCGYGEVGKGCCAALKALGAIV 96
Cdd:cd12154   107 LARAGLTAIAVEGVELPLLTSNSIGAGELSVQFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQV 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  97 YITEIDPICALQACMDG-FRVVKLNEVIRQVDVVITCTGNKN-----VVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRT 170
Cdd:cd12154   187 LITDINVEALEQLEELGgKNVEELEEALAEADVIVTTTLLPGkragiLVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQ 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720403833 171 PELtwervrsqvdhviwpDGKRVVLLAEGRLLNLSC-STVPTFVLSITATTQALALIEL 228
Cdd:cd12154   267 LLE---------------EGHGVVHYGDVNMPGPGCaMGVPWDATLRLAANTLPALVKL 310
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 73-153 2.25e-08

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 52.12  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833   73 VVVCGYGEVGKGCCAALKALGAIVYITEIDP--ICALQACMDG-FRVVKLN-----EVIRQVDVVITC---TGNK--NVV 139
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYSQaelleEAVKEADLVIGAvliPGAKapKLV 102

                           90
                   ....*....|....*
gi 1720403833  140 TREHLDRMK-NSCIV 153
Cdd:smart01002 103 TREMVKSMKpGSVIV 117
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 71-200 8.51e-08

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 52.38  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  71 KQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLN----EV-----IRQVDVVITCTGN--KNVV 139
Cdd:COG0569    96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDatdeEVleeagIEDADAVIAATGDdeANIL 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720403833 140 TrehldrmknsCIVC-NMGHSNTeidVTSLRTPELTWERVRSQVDHVIWPD---GKRVVLLAEGR 200
Cdd:COG0569   176 A----------CLLAkELGVPRI---IARANDPEYADLLERLGADVVISPErlaARRIARLLLRP 227
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 70-155 5.44e-06

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 46.85  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  70 GKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQAcMDGFRVVKLNEVIRQVDVVITCTG----NKNVVTREHLD 145
Cdd:cd05198   140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEE-DLGFRVVSLDELLAQSDVVVLHLPltpeTRHLINEEELA 218

                          90
                  ....*....|
gi 1720403833 146 RMKNSCIVCN 155
Cdd:cd05198   219 LMKPGAVLVN 228
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 70-157 6.65e-06

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 46.75  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  70 GKQVVVCGYGEVGKGCCAALKALGAIVY-----ITEIDPicalqacmDGFRVV---KLNEVIRQVDVVITC------Tgn 135
Cdd:cd05300   134 GKTVLIVGLGDIGREIARRAKAFGMRVIgvrrsGRPAPP--------VVDEVYtpdELDELLPEADYVVNAlpltpeT-- 203

                          90       100
                  ....*....|....*....|..
gi 1720403833 136 KNVVTREHLDRMKNSCIVCNMG 157
Cdd:cd05300   204 RGLFNAERFAAMKPGAVLINVG 225
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 54-146 9.22e-06

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 46.72  E-value: 9.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  54 ESILDGLKrttdvmfgGKQVVVCGYGEVGKGCCAALKALGA-IVYIT----EIdpicALQ-ACMDGFRVV---KLNEVIR 124
Cdd:PRK00045  174 KQIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGVrKITVAnrtlER----AEElAEEFGGEAIpldELPEALA 241

                          90       100
                  ....*....|....*....|...
gi 1720403833 125 QVDVVITCTGNKN-VVTREHLDR 146
Cdd:PRK00045  242 EADIVISSTGAPHpIIGKGMVER 264
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 70-157 1.21e-05

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 44.79  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  70 GKQVVVCGYGEVGKGCCAALKALGA--IVYITEIDPICALQAcmDGFRVVKLNEVIRQVDVV-ITCTGNK---NVVTREH 143
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMkvIAYDRYPKPEEEEEE--LGARYVSLDELLAESDVVsLHLPLTPetrHLINAER 113

                          90
                  ....*....|....
gi 1720403833 144 LDRMKNSCIVCNMG 157
Cdd:pfam02826 114 LALMKPGAILINTA 127
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 73-153 1.43e-05

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 45.18  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  73 VVVCGYGEVGKGCCAALKALGAIVYITEIDP--ICALQACMDG--FRVVKLN-----EVIRQVDVVITC---TGNK--NV 138
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRParLEQLESILGAkfVETLYSQaeliaEAVKEADLVIGTaliPGAKapKL 110

                          90
                  ....*....|....*.
gi 1720403833 139 VTREHLDRMKN-SCIV 153
Cdd:pfam01262 111 VTREMVKSMKPgSVIV 126
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 54-134 2.42e-05

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 44.95  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  54 ESILDGLKrttdvmfgGKQVVVCGYGEVGKGCCAALKALG-AIVYITEIDPICALQ-ACMDGFRVVKLNEV---IRQVDV 128
Cdd:cd05213   170 EKIFGNLK--------GKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEElAKELGGNAVPLDELlelLNEADV 241


                  ....*.
gi 1720403833 129 VITCTG 134
Cdd:cd05213   242 VISATG 247
DpaA COG5842
Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell ...
 70-167 8.77e-05

Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism];


Pssm-ID: 444544 [Multi-domain]  Cd Length: 288  Bit Score: 43.22  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  70 GKQVVVCGYGEVGKGCCAALKALGAIVYITEIDP-----ICALqacmdGFRVV---KLNEVIRQVDVVItctgnkN---- 137
Cdd:COG5842   152 GSNVLVLGFGRCGKTLARKLKALGAKVTVGARKPadlarAYEM-----GYEPVhlsELAEYLGEADIIF------Ntipa 220

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720403833 138 -VVTREHLDRMKNSCIVcnmghsnteIDVTS 167
Cdd:COG5842   221 lVLDAEVLAKLPPDALI---------IDLAS 242
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 54-146 1.01e-04

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 43.18  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  54 ESILDGLKrttdvmfgGKQVVVCGYGEVGKGCCAALKALGA-IVYIT-------EidpicALQACMDGfRVVKLNE---V 122
Cdd:COG0373   174 KKIFGDLS--------GKTVLVIGAGEMGELAARHLAAKGVkRITVAnrtleraE-----ELAEEFGG-EAVPLEElpeA 239

                          90       100
                  ....*....|....*....|....*
gi 1720403833 123 IRQVDVVITCTGNKN-VVTREHLDR 146
Cdd:COG0373   240 LAEADIVISSTGAPHpVITKEMVER 264
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 66-157 1.95e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 42.23  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  66 VMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFrVVKLNEVIRQVDVVITCT----GNKNVVTR 141
Cdd:cd12165   133 KELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGA 211

                          90
                  ....*....|....*.
gi 1720403833 142 EHLDRMKNSCIVCNMG 157
Cdd:cd12165   212 AELAAMKPGAILVNVG 227
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 59-153 2.34e-04

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 41.42  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  59 GLKRTTDVMFG-----GKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQAC-MDGFRVVKLNEVIRQ-VDVVIT 131
Cdd:cd01075    12 GMKAAAEHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAeLFGATVVAPEEIYSVdADVFAP 91

                          90       100
                  ....*....|....*....|..
gi 1720403833 132 CtGNKNVVTREHLDRMKNSCIV 153
Cdd:cd01075    92 C-ALGGVINDDTIPQLKAKAIA 112
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 73-153 4.63e-04

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 41.24  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  73 VVVCGYGEVGKGCCAALKALGAIVYITEIDP--ICALQACMDG-FRVVKLN-----EVIRQVDVVIT---CTGNK--NVV 139
Cdd:cd05305   171 VVILGAGVVGENAARVALGLGAEVTVLDINLerLRYLDDIFGGrVTTLYSNpanleEALKEADLVIGavlIPGAKapKLV 250

                          90
                  ....*....|....*
gi 1720403833 140 TREHLDRMK-NSCIV 153
Cdd:cd05305   251 TEEMVKTMKpGSVIV 265
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 70-135 7.00e-04

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 40.55  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  70 GKQVVVCGYGEVGKGCCAALKALGA-IVYITEIDP-------------ICALQACMDGFRVVKLNEVI--RQVDVVITCT 133
Cdd:cd05285   163 GDTVLVFGAGPIGLLTAAVAKAFGAtKVVVTDIDPsrlefakelgathTVNVRTEDTPESAEKIAELLggKGPDVVIECT 242


                  ..
gi 1720403833 134 GN 135
Cdd:cd05285   243 GA 244
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 54-148 8.87e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 38.71  E-value: 8.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  54 ESILDGLKrttdvmfgGKQVVVCGYGEVGKGCCAALKALGA----IVYITeIDPICALQACMDGFRVVKLNEV---IRQV 126
Cdd:pfam01488   4 KKIFGDLK--------DKKVLLIGAGEMGELVAKHLLAKGAkevtIANRT-IERAQELAEKFGGVEALPLDDLkeyLAEA 74

                          90       100
                  ....*....|....*....|...
gi 1720403833 127 DVVITCTGNKN-VVTREHLDRMK 148
Cdd:pfam01488  75 DIVISATSSPTpIITKEMVERAL 97
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 68-155 8.99e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 40.38  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  68 FGGKQVVVCGYGEVGKGCCAALK-ALGA--IVYiteiDP-ICALQACMDGFRVVKLNEVIRQVDVVITC----TGNKNVV 139
Cdd:cd12177   145 LSGKTVGIIGYGNIGSRVAEILKeGFNAkvLAY----DPyVSEEVIKKKGAKPVSLEELLAESDIISLHapltEETYHMI 220

                          90
                  ....*....|....*.
gi 1720403833 140 TREHLDRMKNSCIVCN 155
Cdd:cd12177   221 NEKAFSKMKKGVILVN 236
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 73-135 1.48e-03

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 37.51  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403833  73 VVVCGYGEVGKGCCAALKAlGAIVYITEIDPICALQACMDGFRVVKLN----EV-----IRQVDVVITCTGN 135
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEELREEGVPVVVGDatdeEVleeagIEEADAVIAATGD 71
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 53-157 1.84e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 39.09  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  53 RESILDGLKRTTDV----MFGGKQVVVCGYGEVGKGCCAALKALGA-IVYIT-----EIDPICAlqacmdGFRVVKLNEV 122
Cdd:cd12175   121 DRELRAGRWGRPEGrpsrELSGKTVGIVGLGNIGRAVARRLRGFGVeVIYYDrfrdpEAEEKDL------GVRYVELDEL 194

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720403833 123 IRQVDVVITCT----GNKNVVTREHLDRMKNSCIVCNMG 157
Cdd:cd12175   195 LAESDVVSLHVpltpETRHLIGAEELAAMKPGAILINTA 233
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 68-149 5.51e-03

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 38.01  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403833  68 FGGKQVVVCGYGEVGKGCCAALKALGAI-VYITE-------------IDPICALQACMDGFRVVKLNEV--IRQVDVVIT 131
Cdd:cd08231   176 GAGDTVVVQGAGPLGLYAVAAAKLAGARrVIVIDgsperlelarefgADATIDIDELPDPQRRAIVRDItgGRGADVVIE 255

                          90
                  ....*....|....*...
gi 1720403833 132 CTGNKNVVtREHLDRMKN 149
Cdd:cd08231   256 ASGHPAAV-PEGLELLRR 272
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 73-140 8.64e-03

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 36.01  E-value: 8.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720403833  73 VVVCGYGEVGKGCCAALKA-----LGAIVyiTEIDPicALQACMDGFRVVKLNEVIRQ---VDVVITCTGNKNVVT 140
Cdd:cd02270     3 VAIVGYGNLGRGVEEAIQAnpdmeLVGVF--RRRDP--KSTKELTPVVVVSVVEHISEldkVDVAILCGGSATDLP 74
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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