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Conserved domains on  [gi|219113257|ref|XP_002186212|]
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predicted protein [Phaeodactylum tricornutum CCAP 1055/1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 1301-1506 5.26e-57

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


:

Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 196.26  E-value: 5.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1301 FNEVSVDlFSFAEAIREAENTGRPIriVLTPTHRSVFDFILLSFLAFSLpelQVDIPFVAAAEDFRQlPIIGWLCSCARA 1380
Cdd:cd07993     1 FDGVQVN-EGQLERLRKAAQEGHPV--VLLPTHRSYLDFLLLSFILFSL---GLPLPHIAAGENLNI-PILGTLLRRLGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1381 IFIRRGTGqVDPDSNQQIQAIGIHRHGPVPVMEVFIEGTRSRDGRFAKPKTGVLKC-----LHQSGIDSLIVPVAISYEA 1455
Cdd:cd07993    74 FFIRRSFG-KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGKLLPPKLGLLSVvveayLKGSVPDVLIVPVSISYDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219113257 1456 IPEQHYMEKELVTGASLKMSTpgaLQWLLDVFDGKNSFGNVLVSAGAPLVM 1506
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESL---SGLLGASKILRENFGRIRVDFGEPISL 200
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 764-1056 7.36e-42

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 cd05236:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 320  Bit Score: 156.69  E-value: 7.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIdTLLENTAVYGFLDKTEKSDLVKV--IEGDVT 841
Cdd:cd05236     1 KSVLITGATGFLGKVLLEKLL--RSCPDIGKIYLLIRGKSGQSAEERL-RELLKDKLFDRGRNLNPLFESKIvpIEGDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  842 RPNALLCKTDLYDVRNDgsISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLAHEKThFVHVSTAFVHGglsgtD 921
Cdd:cd05236    78 EPNLGLSDEDLQTLIEE--VNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKA-FVHVSTAYVNG-----D 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  922 DEPLSERLFPLGsFDANDLYSSMQ--STEFLASKAMRELR-FPNSYTFSKCVCEHLLVKN-SKVRTTIFRPSIVGPACEM 997
Cdd:cd05236   150 RQLIEEKVYPPP-ADPEKLIDILElmDDLELERATPKLLGgHPNTYTFTKALAERLVLKErGNLPLVIVRPSIVGATLKE 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219113257  998 PFEGWAGERPTT---LVAAACLYLSYqwnLWSFGPYRVSCIPVDVVSRFLLSRAFAEGGFRD 1056
Cdd:cd05236   229 PFPGWIDNFNGPdglFLAYGKGILRT---MNADPNAVADIIPVDVVANALLAAAAYSGVRKP 287
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 316-420 3.02e-14

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member cd00616:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 352  Bit Score: 76.04  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  316 VDIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADVVFVSFG 392
Cdd:cd00616    94 IDPELIEAAITPRTKAIIPVHLYGNPA----DMDAIMAIAKRHGLPVIEDAAQ---ALGA-TYKGRKvgtFGDAGAFSFH 165

                          90       100
                  ....*....|....*....|....*...
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLH 420
Cdd:cd00616   166 PTKNLTTGEGGAVVTNDEELAERARLLR 193
ACBP pfam00887
Acyl CoA binding protein;
12-103 2.15e-13

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 66.85  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257    12 QELFDSVVQLIRETPTpddsahQLSTGDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTGLS 91
Cdd:pfam00887    1 EEKFEAAAEFVKKLKS------KPSNEEKLELYGLYK--QATVGDCNTPR--------PGMFDFKGKAKWDAWKKLGGMS 64

                           90
                   ....*....|..
gi 219113257    92 REEAMREYISLL 103
Cdd:pfam00887   65 KEEAMAKYVELV 76
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 1301-1506 5.26e-57

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 196.26  E-value: 5.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1301 FNEVSVDlFSFAEAIREAENTGRPIriVLTPTHRSVFDFILLSFLAFSLpelQVDIPFVAAAEDFRQlPIIGWLCSCARA 1380
Cdd:cd07993     1 FDGVQVN-EGQLERLRKAAQEGHPV--VLLPTHRSYLDFLLLSFILFSL---GLPLPHIAAGENLNI-PILGTLLRRLGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1381 IFIRRGTGqVDPDSNQQIQAIGIHRHGPVPVMEVFIEGTRSRDGRFAKPKTGVLKC-----LHQSGIDSLIVPVAISYEA 1455
Cdd:cd07993    74 FFIRRSFG-KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGKLLPPKLGLLSVvveayLKGSVPDVLIVPVSISYDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219113257 1456 IPEQHYMEKELVTGASLKMSTpgaLQWLLDVFDGKNSFGNVLVSAGAPLVM 1506
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESL---SGLLGASKILRENFGRIRVDFGEPISL 200
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 764-1056 7.36e-42

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 156.69  E-value: 7.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIdTLLENTAVYGFLDKTEKSDLVKV--IEGDVT 841
Cdd:cd05236     1 KSVLITGATGFLGKVLLEKLL--RSCPDIGKIYLLIRGKSGQSAEERL-RELLKDKLFDRGRNLNPLFESKIvpIEGDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  842 RPNALLCKTDLYDVRNDgsISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLAHEKThFVHVSTAFVHGglsgtD 921
Cdd:cd05236    78 EPNLGLSDEDLQTLIEE--VNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKA-FVHVSTAYVNG-----D 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  922 DEPLSERLFPLGsFDANDLYSSMQ--STEFLASKAMRELR-FPNSYTFSKCVCEHLLVKN-SKVRTTIFRPSIVGPACEM 997
Cdd:cd05236   150 RQLIEEKVYPPP-ADPEKLIDILElmDDLELERATPKLLGgHPNTYTFTKALAERLVLKErGNLPLVIVRPSIVGATLKE 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219113257  998 PFEGWAGERPTT---LVAAACLYLSYqwnLWSFGPYRVSCIPVDVVSRFLLSRAFAEGGFRD 1056
Cdd:cd05236   229 PFPGWIDNFNGPdglFLAYGKGILRT---MNADPNAVADIIPVDVVANALLAAAAYSGVRKP 287
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 768-1044 1.05e-40

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 151.22  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   768 LTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFLDKtEKSDLVKVIEGDVTRPNALL 847
Cdd:pfam07993    1 LTGATGFLGKVLLEKLL--RSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLK-EALERIVPVAGDLSEPNLGL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   848 CKTDLYDVRNdgSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLaHEKTHFVHVSTAFVHGGLSGTDDEplse 927
Cdd:pfam07993   78 SEEDFQELAE--EVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQG-KQLKPFHHVSTAYVNGERGGLVEE---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   928 rlfplgsfdanDLYSSMQSTEFLASKAMRELR-FPNSYTFSKCVCEHLLVKNSK--VRTTIFRPSIVGPAcemPFEGWA- 1003
Cdd:pfam07993  151 -----------KPYPEGEDDMLLDEDEPALLGgLPNGYTQTKWLAEQLVREAARrgLPVVIYRPSIITGE---PKTGWIn 216

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 219113257  1004 GERPTTLVAAACLYLSYQWNLWSFGPYRVSCIPVDVVSRFL 1044
Cdd:pfam07993  217 NFDFGPRGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 764-991 1.58e-28

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 116.46  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLLHRKVlgikKVILICRSKRGISAQARIDTLLEntavYGFLDKTEKSDLVKVIEGDVTRP 843
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDA----RVYCLVRASDEAAARERLEALLE----RYGLWLELDASRVVVVAGDLTQP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  844 NALLCKTDLYDVRndGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAAslAHEKTHFVHVSTAFVHGGLSGTdde 923
Cdd:COG3320    73 RLGLSEAEFQELA--EEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAA--TGRLKPFHYVSTIAVAGPADRS--- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  924 plserlfplGSFDANDLYSSMqsteflaskamrelRFPNSYTFSKCVCEHLLVK--NSKVRTTIFRPSIV 991
Cdd:COG3320   146 ---------GVFEEDDLDEGQ--------------GFANGYEQSKWVAEKLVREarERGLPVTIYRPGIV 192
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 1327-1453 7.42e-20

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 86.64  E-value: 7.42e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   1327 IVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDFRqLPIIGWLCSCARAIFIRRGTGQVDPdsnQQIQAIGIHRH 1406
Cdd:smart00563    1 ALVVANHQSFLDPLVLSAL---LPRKLGRVRFVAKKELFY-VPLLGWLLRLLGAIFIDRSNGRKAR---AALREAVELLK 73

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 219113257   1407 GPVPVMeVFIEGTRSRDGRFAKPKTGVLKCLHQSGIdsLIVPVAISY 1453
Cdd:smart00563   74 EGEWLL-IFPEGTRSRPGKLLPFKKGAARLALEAGV--PIVPVAIRG 117
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1287-1453 6.88e-19

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 86.99  E-value: 6.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1287 RCIGFLAKKVLRLCFNEVSVdlfsfaeaiREAENTGRPIRIVLTPTHRSVFDFILLSFLafslpeLQVDIPFVAAAEDFR 1366
Cdd:COG0204    14 RLVRLWARLLLRLLGVRVRV---------EGLENLPADGPVLIVANHQSWLDILLLLAA------LPRPVRFVAKKELFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1367 qLPIIGWLCSCARAIFIRRGTGQVDPDSNQQIQAIgIHRHGPVpVMevFIEGTRSRDGRFAKPKTGVLKCLHQSGIDslI 1446
Cdd:COG0204    79 -IPLLGWLLRALGAIPVDRSKRRAALRALRQAVEA-LKAGESL-VI--FPEGTRSPDGRLLPFKTGAARLALEAGVP--I 151


                  ....*..
gi 219113257 1447 VPVAISY 1453
Cdd:COG0204   152 VPVAIDG 158
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 1286-1504 9.05e-18

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 89.94  E-value: 9.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1286 IRCIGFLAKKVLRLCFNEVSVDLFSFaEAIREAENTGRpIRIVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDF 1365
Cdd:PTZ00374  592 CRLFGLMVRRILFRLYDRVSLNSGAF-ERLHRYVAMPR-VAVVLLPLHRSYIDFIIMTYL---LAVMGLPLPHVCAGDDF 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1366 RQLPIIGWLCSCARAIFIRRgTGQVDPDSNQQIQAIGIHRHGPVPVMEVFIEGTRSRDGRFAKPKTGVLKCL-------H 1438
Cdd:PTZ00374  667 LRMGPIATLMRGSGAFFMRR-SFRDDPLYAALFKEYVRHLVLRRRPLEFFIEGTRSRTGKTMAPKLGLLKFIcdtfyegQ 745

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219113257 1439 QSGIDSLIVPVAISYEAIPEQHYMEKELVtGASLKMSTPGALQWLLDVFdgKNSFGNVLVSAGAPL 1504
Cdd:PTZ00374  746 QELDDVLIIPVSLSYDELLETTLYAKEQL-GVSKPKENPGNLLRARSLL--KRRHGKIHVHIGEPV 808
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 1315-1452 2.52e-16

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 76.93  E-value: 2.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  1315 IREAENTGRPIRIVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDFRqLPIIGWLCSCARAIFIRRGTGQVDPDS 1394
Cdd:pfam01553    4 VHGLENLPRGGPAIVVANHQSYLDVLLLSLA---LYKRGRPLVFVAKKELFD-IPLVGWLMRLLGCIFIDRKNRKDAAGT 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 219113257  1395 NQQI-QAIgihRHGPVpvMEVFIEGTRSRDGRFAKPKTGVLKCLHQSGIdsLIVPVAIS 1452
Cdd:pfam01553   80 LEYLvELL---REGKL--VVIFPEGTRSREGELLPFKKGAFRLAIEAGV--PIVPVAIS 131
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 316-420 3.02e-14

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 76.04  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  316 VDIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADVVFVSFG 392
Cdd:cd00616    94 IDPELIEAAITPRTKAIIPVHLYGNPA----DMDAIMAIAKRHGLPVIEDAAQ---ALGA-TYKGRKvgtFGDAGAFSFH 165

                          90       100
                  ....*....|....*....|....*...
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLH 420
Cdd:cd00616   166 PTKNLTTGEGGAVVTNDEELAERARLLR 193
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
317-420 3.47e-14

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 75.88  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  317 DIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADV-VFvSFG 392
Cdd:COG0399   107 DPEALEAAITPRTKAIIPVHLYGQPA----DMDAIMAIAKKHGLKVIEDAAQ---ALGA-TYKGKKvgtFGDAgCF-SFY 177

                          90       100
                  ....*....|....*....|....*...
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLH 420
Cdd:COG0399   178 PTKNLTTGEGGAVVTNDEELAERARSLR 205
ACBP pfam00887
Acyl CoA binding protein;
12-103 2.15e-13

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 66.85  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257    12 QELFDSVVQLIRETPTpddsahQLSTGDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTGLS 91
Cdd:pfam00887    1 EEKFEAAAEFVKKLKS------KPSNEEKLELYGLYK--QATVGDCNTPR--------PGMFDFKGKAKWDAWKKLGGMS 64

                           90
                   ....*....|..
gi 219113257    92 REEAMREYISLL 103
Cdd:pfam00887   65 KEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 11-104 6.96e-12

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 62.73  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   11 LQELFDSVVQLIRETPTpddsahQLSTGDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTGL 90
Cdd:cd00435     1 LQEEFEAAAEKVKKLKT------KPSNEEKLQLYSLYK--QATVGDCNTER--------PGMFDLKGRAKWDAWNSLKGM 64

                          90
                  ....*....|....
gi 219113257   91 SREEAMREYISLLS 104
Cdd:cd00435    65 SKEDAMKAYIAKVE 78
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 765-1050 1.44e-10

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 64.74  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   765 KVILTGATGFIGSLVLRDLLlhrKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFldkTEKSDLVKVIEGDVTRPN 844
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELL---RRSTRAKVICLVRADSEEHAMERLREALRSYRLWHE---NLAMERIEVVAGDLSKPR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   845 ALLckTDLYDVRNDGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASlaHEKTHFVHVSTAFVhgglsGTDdep 924
Cdd:TIGR01746   75 LGL--SDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAAS--GRAKPLHYVSTISV-----GAA--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   925 lsERLFPLGSFDANDLYSSmqsteflaskamreLRFPNSYTFSKCVCEHLLVK--NSKVRTTIFRPsivGPACEMPFEG- 1001
Cdd:TIGR01746  143 --IDLSTGVTEDDATVTPY--------------PGLAGGYTQSKWVAELLVREasDRGLPVTIVRP---GRILGDSYTGa 203

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 219113257  1002 WAGERPTTLVAAACLYLSYQwnlWSFGPYRVSCIPVDVVSRFLLSRAFA 1050
Cdd:TIGR01746  204 WNSSDILWRMVKGCLALGAY---PQSPELTEDLTPVDFVARAIVALSSR 249
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
10-102 1.93e-10

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   10 SLQELFDSVVQLIRETPTPDDSAhqlstgDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTG 89
Cdd:COG4281     3 DLQAAFEAAVARVKTLTERPDND------TLLKLYALYK--QATEGDVTGKR--------PGMTDFVGRAKYDAWAQLKG 66

                          90
                  ....*....|...
gi 219113257   90 LSREEAMREYISL 102
Cdd:COG4281    67 MSKDEAMQQYIDL 79
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 274-421 2.50e-10

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 64.23  E-value: 2.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   274 IICPPINVPGMLRVLRHHRLEVVGVDLPPSDettrnttttISVDIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKT 353
Cdd:pfam01041   67 VITPSFTFVATANAALRLGAKPVFVDIDPDT---------YNIDPEAIEAAITPRTKAIIPVHLYGQPA----DMDAIRA 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219113257   354 LADQHKLDVMEDCAEiftGLGSlSYRGSPQ---ADVVFVSFGLIKTSTALGGGIAMVKNIKVAETMKRLHF 421
Cdd:pfam01041  134 IAARHGLPVIEDAAH---ALGA-TYQGKKVgtlGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRN 200
PRK07201 PRK07201
SDR family oxidoreductase;
767-991 3.61e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 64.59  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  767 ILTGATGFIGSLVLRDLLLHRKVlgiKKVILICRSkrgiSAQARIDTLLENtavYGfldktekSDLVKVIEGDVTRPNAL 846
Cdd:PRK07201    4 FVTGGTGFIGRRLVSRLLDRRRE---ATVHVLVRR----QSLSRLEALAAY---WG-------ADRVVPLVGDLTEPGLG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  847 LCKTDLYDVrndGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLahEKTHFVHVSTAFVHGGLSGTddepLS 926
Cdd:PRK07201   67 LSEADIAEL---GDIDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERL--QAATFHHVSSIAVAGDYEGV----FR 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219113257  927 ERLFPLGSfdandlyssmqsteflaskamrelRFPNSYTFSKCVCEHLLVKNSKVRTTIFRPSIV 991
Cdd:PRK07201  138 EDDFDEGQ------------------------GLPTPYHRTKFEAEKLVREECGLPWRVYRPAVV 178
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 316-382 3.21e-08

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 57.54  E-value: 3.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219113257  316 VDIEGIEAAITDKTVAILVVHpFGMVSAsnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP 382
Cdd:PRK11706  107 IDETLIEAAITPKTRAIVPVH-YAGVAC---EMDTIMALAKKHNLFVVEDAAQ---GVMS-TYKGRA 165
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 1332-1452 9.70e-07

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 49.65  E-value: 9.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  1332 THRSVFDFILLSFlAFSLPelqvdIPFVAAAEDFrQLPIIGWLCSCARAIFI-RRGTGQVDPDSNQQIQAIGIHRhgpvp 1410
Cdd:TIGR00530   23 NHQSNLDPLTLSA-AFPPP-----IVFIAKKELK-WIPFFGIMLWLTGAIFIdRENIRAIATALKAAIEVLKQGR----- 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 219113257  1411 VMEVFIEGTRSRDGRFAKPKTGVLKCLHQSGIDslIVPVAIS 1452
Cdd:TIGR00530   91 SIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVP--ILPVVLS 130
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 11-104 6.25e-06

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 45.97  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   11 LQELFDSVVQLIRETPtpddSAHQLSTGDKLRLYGLYKhiEASAASDNSDktavdeeaAPSIFRVEAYAKYQALKACTGL 90
Cdd:PTZ00458    1 MADLFEECVSFINSLP----KTVNLSVEIKLDLYKYYK--QSTVGNCNIK--------EPSMFKYQDRKKYEAWKSIENL 66

                          90
                  ....*....|....
gi 219113257   91 SREEAMREYISLLS 104
Cdd:PTZ00458   67 NREDAKKRYVEIVT 80
 
Name Accession Description Interval E-value
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 1301-1506 5.26e-57

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 196.26  E-value: 5.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1301 FNEVSVDlFSFAEAIREAENTGRPIriVLTPTHRSVFDFILLSFLAFSLpelQVDIPFVAAAEDFRQlPIIGWLCSCARA 1380
Cdd:cd07993     1 FDGVQVN-EGQLERLRKAAQEGHPV--VLLPTHRSYLDFLLLSFILFSL---GLPLPHIAAGENLNI-PILGTLLRRLGA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1381 IFIRRGTGqVDPDSNQQIQAIGIHRHGPVPVMEVFIEGTRSRDGRFAKPKTGVLKC-----LHQSGIDSLIVPVAISYEA 1455
Cdd:cd07993    74 FFIRRSFG-KDPLYRAVLQEYVQELLKNGQPLEFFIEGTRSRTGKLLPPKLGLLSVvveayLKGSVPDVLIVPVSISYDR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 219113257 1456 IPEQHYMEKELVTGASLKMSTpgaLQWLLDVFDGKNSFGNVLVSAGAPLVM 1506
Cdd:cd07993   153 VLEEELYAEELLGPPKPKESL---SGLLGASKILRENFGRIRVDFGEPISL 200
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 764-1056 7.36e-42

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 156.69  E-value: 7.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIdTLLENTAVYGFLDKTEKSDLVKV--IEGDVT 841
Cdd:cd05236     1 KSVLITGATGFLGKVLLEKLL--RSCPDIGKIYLLIRGKSGQSAEERL-RELLKDKLFDRGRNLNPLFESKIvpIEGDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  842 RPNALLCKTDLYDVRNDgsISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLAHEKThFVHVSTAFVHGglsgtD 921
Cdd:cd05236    78 EPNLGLSDEDLQTLIEE--VNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKA-FVHVSTAYVNG-----D 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  922 DEPLSERLFPLGsFDANDLYSSMQ--STEFLASKAMRELR-FPNSYTFSKCVCEHLLVKN-SKVRTTIFRPSIVGPACEM 997
Cdd:cd05236   150 RQLIEEKVYPPP-ADPEKLIDILElmDDLELERATPKLLGgHPNTYTFTKALAERLVLKErGNLPLVIVRPSIVGATLKE 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219113257  998 PFEGWAGERPTT---LVAAACLYLSYqwnLWSFGPYRVSCIPVDVVSRFLLSRAFAEGGFRD 1056
Cdd:cd05236   229 PFPGWIDNFNGPdglFLAYGKGILRT---MNADPNAVADIIPVDVVANALLAAAAYSGVRKP 287
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 768-1044 1.05e-40

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 151.22  E-value: 1.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   768 LTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFLDKtEKSDLVKVIEGDVTRPNALL 847
Cdd:pfam07993    1 LTGATGFLGKVLLEKLL--RSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLK-EALERIVPVAGDLSEPNLGL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   848 CKTDLYDVRNdgSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLaHEKTHFVHVSTAFVHGGLSGTDDEplse 927
Cdd:pfam07993   78 SEEDFQELAE--EVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQG-KQLKPFHHVSTAYVNGERGGLVEE---- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   928 rlfplgsfdanDLYSSMQSTEFLASKAMRELR-FPNSYTFSKCVCEHLLVKNSK--VRTTIFRPSIVGPAcemPFEGWA- 1003
Cdd:pfam07993  151 -----------KPYPEGEDDMLLDEDEPALLGgLPNGYTQTKWLAEQLVREAARrgLPVVIYRPSIITGE---PKTGWIn 216

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 219113257  1004 GERPTTLVAAACLYLSYQWNLWSFGPYRVSCIPVDVVSRFL 1044
Cdd:pfam07993  217 NFDFGPRGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 764-991 1.58e-28

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 116.46  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLLHRKVlgikKVILICRSKRGISAQARIDTLLEntavYGFLDKTEKSDLVKVIEGDVTRP 843
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDA----RVYCLVRASDEAAARERLEALLE----RYGLWLELDASRVVVVAGDLTQP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  844 NALLCKTDLYDVRndGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAAslAHEKTHFVHVSTAFVHGGLSGTdde 923
Cdd:COG3320    73 RLGLSEAEFQELA--EEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAA--TGRLKPFHYVSTIAVAGPADRS--- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  924 plserlfplGSFDANDLYSSMqsteflaskamrelRFPNSYTFSKCVCEHLLVK--NSKVRTTIFRPSIV 991
Cdd:COG3320   146 ---------GVFEEDDLDEGQ--------------GFANGYEQSKWVAEKLVREarERGLPVTIYRPGIV 192
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 766-1091 1.51e-22

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 99.75  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  766 VILTGATGFIGSLVLRDLLLhrkvlGIKKVILICRSKRGISAQARIDTLlentavygfldkTEKSDLVKVIEGDVTRPNA 845
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLE-----NGFKVLVLVRSESLGEAHERIEEA------------GLEADRVRVLEGDLTQPNL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  846 LLCKTDLYDVRndGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLahEKTHFVHVSTAFVHGGLSGTDDEPL 925
Cdd:cd05263    64 GLSAAASRELA--GKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARL--DIQRFHYVSTAYVAGNREGNIRETE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  926 SErlfplgsfdandlyssmQSTEflaskamrelrFPNSYTFSKCVCEHLLVKNSK-VRTTIFRPSIV-GPACEMPFEGWA 1003
Cdd:cd05263   140 LN-----------------PGQN-----------FKNPYEQSKAEAEQLVRAAATqIPLTVYRPSIVvGDSKTGRIEKID 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1004 GerPTTLVAAACLYLSYQWnLWSFGPYRVSCIPVDVVSRFLLSRAFAEGGFRDVVGVYDSSSDEDFEKVSCASSALADTV 1083
Cdd:cd05263   192 G--LYELLNLLAKLGRWLP-MPGNKGARLNLVPVDYVADAIVYLSKKPEANGQIFHLTDPTPQTLREIADLFKSAFLSPG 268


                  ....*...
gi 219113257 1084 YAGDPESS 1091
Cdd:cd05263   269 LLVLLMNE 276
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 1327-1453 7.42e-20

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 86.64  E-value: 7.42e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   1327 IVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDFRqLPIIGWLCSCARAIFIRRGTGQVDPdsnQQIQAIGIHRH 1406
Cdd:smart00563    1 ALVVANHQSFLDPLVLSAL---LPRKLGRVRFVAKKELFY-VPLLGWLLRLLGAIFIDRSNGRKAR---AALREAVELLK 73

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 219113257   1407 GPVPVMeVFIEGTRSRDGRFAKPKTGVLKCLHQSGIdsLIVPVAISY 1453
Cdd:smart00563   74 EGEWLL-IFPEGTRSRPGKLLPFKKGAARLALEAGV--PIVPVAIRG 117
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1287-1453 6.88e-19

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 86.99  E-value: 6.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1287 RCIGFLAKKVLRLCFNEVSVdlfsfaeaiREAENTGRPIRIVLTPTHRSVFDFILLSFLafslpeLQVDIPFVAAAEDFR 1366
Cdd:COG0204    14 RLVRLWARLLLRLLGVRVRV---------EGLENLPADGPVLIVANHQSWLDILLLLAA------LPRPVRFVAKKELFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1367 qLPIIGWLCSCARAIFIRRGTGQVDPDSNQQIQAIgIHRHGPVpVMevFIEGTRSRDGRFAKPKTGVLKCLHQSGIDslI 1446
Cdd:COG0204    79 -IPLLGWLLRALGAIPVDRSKRRAALRALRQAVEA-LKAGESL-VI--FPEGTRSPDGRLLPFKTGAARLALEAGVP--I 151


                  ....*..
gi 219113257 1447 VPVAISY 1453
Cdd:COG0204   152 VPVAIDG 158
PlsB COG2937
Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate ...
 1291-1527 1.12e-18

Glycerol-3-phosphate O-acyltransferase [Lipid transport and metabolism]; Glycerol-3-phosphate O-acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 442180 [Multi-domain]  Cd Length: 707  Bit Score: 92.29  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1291 FLAKKVLRLCFNEV--SVDLFSFaEAIREAeNTGRPIriVLTPTHRSVFDFILLSFLAF--SLPelqvdIPFVAAAEDFR 1366
Cdd:COG2937   171 RFLDRVLRWLWNRLydGIRVDNL-ERLREL-AKGHEI--VYVPCHRSHMDYLLLSYVLYhnGLV-----PPHIAAGINLN 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1367 qLPIIGWLcscAR---AIFIRRGTGqvdpdSN-----------QQIQAIGIHrhgpvpvMEVFIEGTRSRDGRFAKPKTG 1432
Cdd:COG2937   242 -FWPLGPI---LRrggAFFIRRSFK-----GNklysavfreylAELFERGYS-------VEYFIEGGRSRTGRLLPPKTG 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1433 VLK-----CLHQSGIDSLIVPVAISYEAIPEQHYMEKELVTGASLKMSTPG---ALQWLldvfdgKNSFGNVLVSAGAPL 1504
Cdd:COG2937   306 MLSmtvqaFLRGARRPVVFVPVYIGYERVLEVGSYAKELRGGEKKKESLGGllrALRKL------RRRFGRVYVNFGEPI 379

                         250       260
                  ....*....|....*....|...
gi 219113257 1505 VMNAAEKTNFKElvWSIQGRQRD 1527
Cdd:COG2937   380 SLSEYLDQHVPD--WRESEDLRP 400
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 765-1049 6.32e-18

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 86.17  E-value: 6.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  765 KVILTGATGFIGSLVLRDLLlhrKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFLDKteKSDLVKVIEGDVTRPN 844
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELL---KRKNVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDEL--ELSRIKVVVGDLSKPN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  845 ALLCKTDLYDVRNDgsISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAaslAHEKTH-FVHVSTAFVhggLSGTDDE 923
Cdd:cd05235    76 LGLSDDDYQELAEE--VDVIIHNGANVNWVYPYEELKPANVLGTKELLKLA---ATGKLKpLHFVSTLSV---FSAEEYN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  924 PLSErlfplgSFDANDLYSSMQSteflaskamrelrfPNSYTFSKCVCEHLLVKNSK--VRTTIFRPSIVGPAcempfeG 1001
Cdd:cd05235   148 ALDD------EESDDMLESQNGL--------------PNGYIQSKWVAEKLLREAANrgLPVAIIRPGNIFGD------S 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 219113257 1002 WAGERPT----TLVAAACLYLSYQWNLWsfgpYRVSCIPVDVVSRFLLSRAF 1049
Cdd:cd05235   202 ETGIGNTddffWRLLKGCLQLGIYPISG----APLDLSPVDWVARAIVKLAL 249
PTZ00374 PTZ00374
dihydroxyacetone phosphate acyltransferase; Provisional
 1286-1504 9.05e-18

dihydroxyacetone phosphate acyltransferase; Provisional


Pssm-ID: 240389 [Multi-domain]  Cd Length: 1108  Bit Score: 89.94  E-value: 9.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1286 IRCIGFLAKKVLRLCFNEVSVDLFSFaEAIREAENTGRpIRIVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDF 1365
Cdd:PTZ00374  592 CRLFGLMVRRILFRLYDRVSLNSGAF-ERLHRYVAMPR-VAVVLLPLHRSYIDFIIMTYL---LAVMGLPLPHVCAGDDF 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1366 RQLPIIGWLCSCARAIFIRRgTGQVDPDSNQQIQAIGIHRHGPVPVMEVFIEGTRSRDGRFAKPKTGVLKCL-------H 1438
Cdd:PTZ00374  667 LRMGPIATLMRGSGAFFMRR-SFRDDPLYAALFKEYVRHLVLRRRPLEFFIEGTRSRTGKTMAPKLGLLKFIcdtfyegQ 745

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219113257 1439 QSGIDSLIVPVAISYEAIPEQHYMEKELVtGASLKMSTPGALQWLLDVFdgKNSFGNVLVSAGAPL 1504
Cdd:PTZ00374  746 QELDDVLIIPVSLSYDELLETTLYAKEQL-GVSKPKENPGNLLRARSLL--KRRHGKIHVHIGEPV 808
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 1293-1453 3.89e-17

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 81.16  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1293 AKKVLRLCFNEVSVdlfsfaeaiREAENTGRPIRIVLTPTHRSVFDFILLSFLafslpeLQVDIPFVAAAEDFRqLPIIG 1372
Cdd:cd07989     1 LRLLLRLLGVRVRV---------EGLENLPPKGPVIIVANHQSYLDPLVLGAA------LPRPIRFVAKKELFK-IPFLG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1373 WLCSCARAIFIRRGTGQVDPDSNQQIQAIgIHRHGPVpVmeVFIEGTRSRDGRFAKPKTGVLKCLHQSGIDslIVPVAIS 1452
Cdd:cd07989    65 WLLRLLGAIPIDRGNGRSAREALREAIEA-LKEGESV-V--IFPEGTRSRDGELLPFKSGAFRLAKEAGVP--IVPVAIS 138


                  .
gi 219113257 1453 Y 1453
Cdd:cd07989   139 G 139
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 1315-1452 2.52e-16

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 76.93  E-value: 2.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  1315 IREAENTGRPIRIVLTPTHRSVFDFILLSFLafsLPELQVDIPFVAAAEDFRqLPIIGWLCSCARAIFIRRGTGQVDPDS 1394
Cdd:pfam01553    4 VHGLENLPRGGPAIVVANHQSYLDVLLLSLA---LYKRGRPLVFVAKKELFD-IPLVGWLMRLLGCIFIDRKNRKDAAGT 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 219113257  1395 NQQI-QAIgihRHGPVpvMEVFIEGTRSRDGRFAKPKTGVLKCLHQSGIdsLIVPVAIS 1452
Cdd:pfam01553   80 LEYLvELL---REGKL--VVIFPEGTRSREGELLPFKKGAFRLAIEAGV--PIVPVAIS 131
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 316-420 3.02e-14

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 76.04  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  316 VDIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADVVFVSFG 392
Cdd:cd00616    94 IDPELIEAAITPRTKAIIPVHLYGNPA----DMDAIMAIAKRHGLPVIEDAAQ---ALGA-TYKGRKvgtFGDAGAFSFH 165

                          90       100
                  ....*....|....*....|....*...
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLH 420
Cdd:cd00616   166 PTKNLTTGEGGAVVTNDEELAERARLLR 193
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
317-420 3.47e-14

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 75.88  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  317 DIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADV-VFvSFG 392
Cdd:COG0399   107 DPEALEAAITPRTKAIIPVHLYGQPA----DMDAIMAIAKKHGLKVIEDAAQ---ALGA-TYKGKKvgtFGDAgCF-SFY 177

                          90       100
                  ....*....|....*....|....*...
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLH 420
Cdd:COG0399   178 PTKNLTTGEGGAVVTNDEELAERARSLR 205
ACBP pfam00887
Acyl CoA binding protein;
12-103 2.15e-13

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 66.85  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257    12 QELFDSVVQLIRETPTpddsahQLSTGDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTGLS 91
Cdd:pfam00887    1 EEKFEAAAEFVKKLKS------KPSNEEKLELYGLYK--QATVGDCNTPR--------PGMFDFKGKAKWDAWKKLGGMS 64

                           90
                   ....*....|..
gi 219113257    92 REEAMREYISLL 103
Cdd:pfam00887   65 KEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 11-104 6.96e-12

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 62.73  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   11 LQELFDSVVQLIRETPTpddsahQLSTGDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTGL 90
Cdd:cd00435     1 LQEEFEAAAEKVKKLKT------KPSNEEKLQLYSLYK--QATVGDCNTER--------PGMFDLKGRAKWDAWNSLKGM 64

                          90
                  ....*....|....
gi 219113257   91 SREEAMREYISLLS 104
Cdd:cd00435    65 SKEDAMKAYIAKVE 78
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
765-993 1.59e-11

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 66.93  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  765 KVILTGATGFIGSLVLRDLLL--HRkvlgikkVILICRSKrgiSAQARIDTLlentavygfldkteksDLVKVIEGDVTR 842
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLArgHE-------VVGLDRSP---PGAANLAAL----------------PGVEFVRGDLRD 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  843 PNALlcKTDLYDVrndgsiSHLIHCAASVSFTQSLPAA-------ATANIssplylqdLAASLAHEKTHFVHVSTAFVHg 915
Cdd:COG0451    55 PEAL--AAALAGV------DAVVHLAAPAGVGEEDPDEtlevnveGTLNL--------LEAARAAGVKRFVYASSSSVY- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  916 glsGTDDEPLSERLfplgsfdandlyssmqsteflaskamrELRFPNSYTFSKCVCEHLL---VKNSKVRTTIFRPS-IV 991
Cdd:COG0451   118 ---GDGEGPIDEDT---------------------------PLRPVSPYGASKLAAELLArayARRYGLPVTILRPGnVY 167


                  ..
gi 219113257  992 GP 993
Cdd:COG0451   168 GP 169
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 765-1050 1.44e-10

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 64.74  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   765 KVILTGATGFIGSLVLRDLLlhrKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFldkTEKSDLVKVIEGDVTRPN 844
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELL---RRSTRAKVICLVRADSEEHAMERLREALRSYRLWHE---NLAMERIEVVAGDLSKPR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   845 ALLckTDLYDVRNDGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASlaHEKTHFVHVSTAFVhgglsGTDdep 924
Cdd:TIGR01746   75 LGL--SDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAAS--GRAKPLHYVSTISV-----GAA--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   925 lsERLFPLGSFDANDLYSSmqsteflaskamreLRFPNSYTFSKCVCEHLLVK--NSKVRTTIFRPsivGPACEMPFEG- 1001
Cdd:TIGR01746  143 --IDLSTGVTEDDATVTPY--------------PGLAGGYTQSKWVAELLVREasDRGLPVTIVRP---GRILGDSYTGa 203

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 219113257  1002 WAGERPTTLVAAACLYLSYQwnlWSFGPYRVSCIPVDVVSRFLLSRAFA 1050
Cdd:TIGR01746  204 WNSSDILWRMVKGCLALGAY---PQSPELTEDLTPVDFVARAIVALSSR 249
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
10-102 1.93e-10

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   10 SLQELFDSVVQLIRETPTPDDSAhqlstgDKLRLYGLYKhiEASAASDNSDKtavdeeaaPSIFRVEAYAKYQALKACTG 89
Cdd:COG4281     3 DLQAAFEAAVARVKTLTERPDND------TLLKLYALYK--QATEGDVTGKR--------PGMTDFVGRAKYDAWAQLKG 66

                          90
                  ....*....|...
gi 219113257   90 LSREEAMREYISL 102
Cdd:COG4281    67 MSKDEAMQQYIDL 79
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 274-421 2.50e-10

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 64.23  E-value: 2.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   274 IICPPINVPGMLRVLRHHRLEVVGVDLPPSDettrnttttISVDIEGIEAAITDKTVAILVVHPFGMVSasnrDFERIKT 353
Cdd:pfam01041   67 VITPSFTFVATANAALRLGAKPVFVDIDPDT---------YNIDPEAIEAAITPRTKAIIPVHLYGQPA----DMDAIRA 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219113257   354 LADQHKLDVMEDCAEiftGLGSlSYRGSPQ---ADVVFVSFGLIKTSTALGGGIAMVKNIKVAETMKRLHF 421
Cdd:pfam01041  134 IAARHGLPVIEDAAH---ALGA-TYQGKKVgtlGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRN 200
PRK07201 PRK07201
SDR family oxidoreductase;
767-991 3.61e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 64.59  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  767 ILTGATGFIGSLVLRDLLLHRKVlgiKKVILICRSkrgiSAQARIDTLLENtavYGfldktekSDLVKVIEGDVTRPNAL 846
Cdd:PRK07201    4 FVTGGTGFIGRRLVSRLLDRRRE---ATVHVLVRR----QSLSRLEALAAY---WG-------ADRVVPLVGDLTEPGLG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  847 LCKTDLYDVrndGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLahEKTHFVHVSTAFVHGGLSGTddepLS 926
Cdd:PRK07201   67 LSEADIAEL---GDIDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERL--QAATFHHVSSIAVAGDYEGV----FR 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219113257  927 ERLFPLGSfdandlyssmqsteflaskamrelRFPNSYTFSKCVCEHLLVKNSKVRTTIFRPSIV 991
Cdd:PRK07201  138 EDDFDEGQ------------------------GLPTPYHRTKFEAEKLVREECGLPWRVYRPAVV 178
PRK04974 PRK04974
glycerol-3-phosphate 1-O-acyltransferase PlsB;
1312-1507 6.05e-10

glycerol-3-phosphate 1-O-acyltransferase PlsB;


Pssm-ID: 235325 [Multi-domain]  Cd Length: 818  Bit Score: 64.10  E-value: 6.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1312 AEAIREAENTGRpiRIVLTPTHRSVFDFILLSFLAFS---LPelqvdiPFVAAAEDFrQLPIIGWLCSCARAIFIRR--- 1385
Cdd:PRK04974  291 AERVRQLAQDGH--EIVYVPCHRSHMDYLLLSYVLYHqglVP------PHIAAGINL-NFWPAGPIFRRGGAFFIRRsfk 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1386 GtgqvdpdsNQQIQAIG-------IHRHGPVpvmEVFIEGTRSRDGRFAKPKTGVL-----KCLHQSGIDSLIVPVAISY 1453
Cdd:PRK04974  362 G--------NKLYSTVFreylgelFARGYSV---EYFVEGGRSRTGRLLQPKTGMLamtlqAMLRGSRRPITLVPVYIGY 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219113257 1454 EaipeqHYME-----KELvTGASLKmsTPGALQwLLDVFDGKNSFGNVLVSAGAPLVMN 1507
Cdd:PRK04974  431 E-----HVMEvgtyaKEL-RGAPKE--KESLFQ-VLRGIRKLRNFGQGYVNFGEPIPLN 480
PLN02996 PLN02996
fatty acyl-CoA reductase
 763-1040 1.32e-09

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 62.42  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  763 ERKVIL-TGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIDT----------LLENtavYGFLDKTEKSD 831
Cdd:PLN02996   10 ENKTILvTGATGFLAKIFVEKIL--RVQPNVKKLYLLLRASDAKSATQRLHDevigkdlfkvLREK---LGENLNSLISE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  832 LVKVIEGDVTRPNALLCKTDLYDvRNDGSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLAHEKThFVHVSTA 911
Cdd:PLN02996   85 KVTPVPGDISYDDLGVKDSNLRE-EMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKM-LLHVSTA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  912 FVHGGLSGTddepLSERLFPLG-------SFDANDLYSSMQ----------STEFLASKAMRELR--------FPNSYTF 966
Cdd:PLN02996  163 YVCGEKSGL----ILEKPFHMGetlngnrKLDINEEKKLVKeklkelneqdASEEEITQAMKDLGmeraklhgWPNTYVF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  967 SKCVCEHLLV-KNSKVRTTIFRPSIVGPACEMPFEGW-AGERPTTLVAAAclylsyqwnlwsFGPYRVSC---------- 1034
Cdd:PLN02996  239 TKAMGEMLLGnFKENLPLVIIRPTMITSTYKEPFPGWiEGLRTIDSVIVG------------YGKGKLTCfladpnsvld 306


                  ....*..
gi 219113257 1035 -IPVDVV 1040
Cdd:PLN02996  307 vIPADMV 313
PRK03355 PRK03355
glycerol-3-phosphate 1-O-acyltransferase;
1303-1506 3.61e-09

glycerol-3-phosphate 1-O-acyltransferase;


Pssm-ID: 179567 [Multi-domain]  Cd Length: 783  Bit Score: 61.65  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1303 EVSVDLFSFAEaIREA-ENTGrpirIVLTPTHRSVFDFILLS--FLAFSLPELQVdipFVAAAEDFRqlpIIGWLCSCAR 1379
Cdd:PRK03355  249 EIDYDEYELAA-LRALlEEHP----AVLLFSHRSYIDGLVVPvaMQENRLPPVHV---FGGINLSFG---PMGPIMRRSG 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1380 AIFIRRGTGqvdpdsNQQIQAIGIHRHGPVPV-----MEVFIEGTRSRDGRFAKPKTGVLKCL----HQSGI-DSLIVPV 1449
Cdd:PRK03355  318 MIFIRRNIG------DDPLYKYVLREYVGYLVekrfnLSWYIEGTRSRTGKLLPPKLGLLSYVadayLDGRSdDVLLQPV 391

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219113257 1450 AISYEAIPEQHYMEKELVTGAslkmSTPGALQWLLDVF--DGKNSFGNVLVSAGAPLVM 1506
Cdd:PRK03355  392 SISFDQLHEIGEYAAEARGGE----KTPEGLRWLYNYIkaQGERNYGKIYVRFGEPVSM 446
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 316-382 3.21e-08

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 57.54  E-value: 3.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219113257  316 VDIEGIEAAITDKTVAILVVHpFGMVSAsnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP 382
Cdd:PRK11706  107 IDETLIEAAITPKTRAIVPVH-YAGVAC---EMDTIMALAKKHNLFVVEDAAQ---GVMS-TYKGRA 165
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 760-991 3.74e-08

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 58.54  E-value: 3.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   760 SPCERKVILTGATGFIGSLVLRDLLLHRKVLGIkKVILICRSKrgiSAQARIDTLLENTAVYGFLDKTEKSDLvKVIEGD 839
Cdd:TIGR03443  968 ASTPITVFLTGATGFLGSFILRDLLTRRSNSNF-KVFAHVRAK---SEEAGLERLRKTGTTYGIWDEEWASRI-EVVLGD 1042

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   840 VTRPNALLCKTDLYDVRNdgSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASlAHEKT-------------HFV 906
Cdd:TIGR03443 1043 LSKEKFGLSDEKWSDLTN--EVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAE-GKAKQfsfvsstsaldteYYV 1119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   907 HVSTAFVHGGLSGtddepLSErlfplgsfdANDLYSSmqsteflaSKAMRelrfpNSYTFSKCVCEHLLVKNSK--VRTT 984
Cdd:TIGR03443 1120 NLSDELVQAGGAG-----IPE---------SDDLMGS--------SKGLG-----TGYGQSKWVAEYIIREAGKrgLRGC 1172


                   ....*..
gi 219113257   985 IFRPSIV 991
Cdd:TIGR03443 1173 IVRPGYV 1179
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
316-421 4.33e-08

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 57.34  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  316 VDIEGIEAAITDKTVAILVVHPFGmvsaSNRDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSP---QADVVFvSFG 392
Cdd:PRK11658  109 VTPEAIEAAITPRTKAIIPVHYAG----APADLDAIRAIGERYGIPVIEDAAH---AVGT-YYKGRHigaRGTAIF-SFH 179

                          90       100
                  ....*....|....*....|....*....
gi 219113257  393 LIKTSTALGGGIAMVKNIKVAETMKRLHF 421
Cdd:PRK11658  180 AIKNITCAEGGLVVTDDDELADRLRSLKF 208
PLN02503 PLN02503
fatty acyl-CoA reductase 2
 764-1002 7.43e-08

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 57.18  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILICRSKRGISAQARIDTLLENTAVYGFLDKTEKSD--------LVKV 835
Cdd:PLN02503  120 KNFLITGATGFLAKVLIEKIL--RTNPDVGKIYLLIKAKDKEAAIERLKNEVIDAELFKCLQETHGKSyqsfmlskLVPV 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  836 IeGDVTRPNALLCKtDLYDVRNDgSISHLIHCAASVSFTQSLPAAATANISSPLYLQDLAASLAHEKThFVHVSTAFVHG 915
Cdd:PLN02503  198 V-GNVCESNLGLEP-DLADEIAK-EVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKL-FLQVSTAYVNG 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  916 GLSGTddepLSERLFPLGSFDANDLYSS--------------------------MQSTEFlaSKAMREL--------RFP 961
Cdd:PLN02503  274 QRQGR----IMEKPFRMGDCIARELGISnslphnrpaldieaeiklaldskrhgFQSNSF--AQKMKDLgleraklyGWQ 347

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 219113257  962 NSYTFSKCVCEhlLVKNS---KVRTTIFRPSIVGPACEMPFEGW 1002
Cdd:PLN02503  348 DTYVFTKAMGE--MVINSmrgDIPVVIIRPSVIESTWKDPFPGW 389
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 766-1002 1.13e-07

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 53.84  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  766 VILTGATGFIGSLVLRDLLLHrkvlGIKkvilicrskrgisaqaridtllentaVYGFldkteksdlvkviegdvtrpna 845
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLER----GHE--------------------------VVVI---------------------- 28

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  846 llcktDLYDVrndgsishLIHCAASVSFTQSLP---AAATANISSPLYLQDLAAslAHEKTHFVHVSTAFVHGGLSGTDD 922
Cdd:cd08946    29 -----DRLDV--------VVHLAALVGVPASWDnpdEDFETNVVGTLNLLEAAR--KAGVKRFVYASSASVYGSPEGLPE 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  923 EPlSERLFPLgsfdandlyssmqsteflaskamrelrfpNSYTFSKCVCEHLLV---KNSKVRTTIFRPSIV-GPACEMP 998
Cdd:cd08946    94 EE-ETPPRPL-----------------------------SPYGVSKLAAEHLLRsygESYGLPVVILRLANVyGPGQRPR 143


                  ....
gi 219113257  999 FEGW 1002
Cdd:cd08946   144 LDGV 147
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
 764-993 6.06e-07

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 53.32  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILicrskrgisaqariDTL-----LENtavygfLDKTEKSDLVKVIEG 838
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLL--NKYPDYKIINL--------------DKLtyagnLEN------LEDVSSSPRYRFVKG 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  839 DVTRPNAL--LCKTDLYDVrndgsishLIHCAASV----SFTQSLPAAATaNISSPLYLqdLAASLAHEKTHFVHVSTAF 912
Cdd:cd05246    59 DICDAELVdrLFEEEKIDA--------VIHFAAEShvdrSISDPEPFIRT-NVLGTYTL--LEAARKYGVKRFVHISTDE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  913 VHGGLSGTddeplserlfplGSFDANDLYSsmqsteflaskamrelrfPNS-YTFSKCVCEHLL---VKNSKVRTTIFRP 988
Cdd:cd05246   128 VYGDLLDD------------GEFTETSPLA------------------PTSpYSASKAAADLLVrayHRTYGLPVVITRC 177


                  ....*.
gi 219113257  989 S-IVGP 993
Cdd:cd05246   178 SnNYGP 183
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 1332-1452 9.70e-07

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 49.65  E-value: 9.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  1332 THRSVFDFILLSFlAFSLPelqvdIPFVAAAEDFrQLPIIGWLCSCARAIFI-RRGTGQVDPDSNQQIQAIGIHRhgpvp 1410
Cdd:TIGR00530   23 NHQSNLDPLTLSA-AFPPP-----IVFIAKKELK-WIPFFGIMLWLTGAIFIdRENIRAIATALKAAIEVLKQGR----- 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 219113257  1411 VMEVFIEGTRSRDGRFAKPKTGVLKCLHQSGIDslIVPVAIS 1452
Cdd:TIGR00530   91 SIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVP--ILPVVLS 130
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 1311-1454 1.92e-06

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 50.11  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1311 FAEAIREAENTGRPIriVLTPTHRSVFDFILLSFLAFSLPElqVDIPFVAAAEDFRQLPIIGWLcscaRAIFIRRGTGQV 1390
Cdd:cd06551    14 LEVKGPPPPPGGGPV--LFVSNHSSWWDGLILFLLLERGLR--RDVYGLMDEELLERYPFFTRL----GAFSVDRDSPRS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219113257 1391 DPDSNQQIQAIgIHRHGPVPVMevFIEGTRSRDGRFAK-PKTGVLKCLHQSGIDslIVPVAISYE 1454
Cdd:cd06551    86 AAKSLKYVARL-LSKPGSVVWI--FPEGTRTRRDKRPLqFKPGVAHLAEKAGVP--IVPVALRYT 145
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 316-397 2.89e-06

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 51.81  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  316 VDIEGIEAAITDKTVAILVVH----PFgmvsasnrDFERIKTLADQHKLDVMEDCAEiftGLGSlSYRGSpqadvvFV-S 390
Cdd:PRK15407  147 IDASLLEAAVSPKTKAIMIAHtlgnPF--------DLAAVKAFCDKHNLWLIEDNCD---ALGS-TYDGR------MTgT 208


                  ....*..
gi 219113257  391 FGLIKTS 397
Cdd:PRK15407  209 FGDIATL 215
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 233-420 3.98e-06

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 50.80  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  233 QWIRGMEGDGQSPQNVVVGLAVRSLLdlYLLSRSF-PEGSQIIICPPiNVPGMLRVLRHHRLEVVGVDLPPSDettrntt 311
Cdd:cd00609    47 EWLGRRGGVDVPPEEIVVTNGAQEAL--SLLLRALlNPGDEVLVPDP-TYPGYEAAARLAGAEVVPVPLDEEG------- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  312 tTISVDIEGIEAAITDKTVAILVVH---PFGMVsASNRDFERIKTLADQHKLDVMEDcaEIFtglGSLSYRGSP------ 382
Cdd:cd00609   117 -GFLLDLELLEAAKTPKTKLLYLNNpnnPTGAV-LSEEELEELAELAKKHGILIISD--EAY---AELVYDGEPppalal 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 219113257  383 --QADVVFVSFGLIKTS--TALGGGIAMVKNIKVAETMKRLH 420
Cdd:cd00609   190 ldAYERVIVLRSFSKTFglPGLRIGYLIAPPEELLERLKKLL 231
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 11-104 6.25e-06

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 45.97  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   11 LQELFDSVVQLIRETPtpddSAHQLSTGDKLRLYGLYKhiEASAASDNSDktavdeeaAPSIFRVEAYAKYQALKACTGL 90
Cdd:PTZ00458    1 MADLFEECVSFINSLP----KTVNLSVEIKLDLYKYYK--QSTVGNCNIK--------EPSMFKYQDRKKYEAWKSIENL 66

                          90
                  ....*....|....
gi 219113257   91 SREEAMREYISLLS 104
Cdd:PTZ00458   67 NREDAKKRYVEIVT 80
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 766-971 1.94e-05

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 46.63  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  766 VILTGATGFIGSLVLRDLLlhrkvLGIKKVILICRSKRGISAQARidtllentavygfldkteksDLVKVIEGDVTRPNA 845
Cdd:cd05226     1 ILILGATGFIGRALARELL-----EQGHEVTLLVRNTKRLSKEDQ--------------------EPVAVVEGDLRDLDS 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  846 LLcktdlyDVRNDgsISHLIHCAASVSFTQslpAAATANISSPLYLqdLAASLAHEKTHFVHVSTAFVHGGLSGTDDEPL 925
Cdd:cd05226    56 LS------DAVQG--VDVVIHLAGAPRDTR---DFCEVDVEGTRNV--LEAAKEAGVKHFIFISSLGAYGDLHEETEPSP 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 219113257  926 SERLFPlgsfdandlysSMQSTEflasKAMRELRFPnsYTFSKCVC 971
Cdd:cd05226   123 SSPYLA-----------VKAKTE----AVLREASLP--YTIVRPGV 151
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 766-957 2.18e-05

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 47.68  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   766 VILTGATGFIGSLVLRDLLLH-RKVLGIkkvilicrsKRGISAqaridtllentavygflDKTEKSDLVKVIEGDVTRPN 844
Cdd:pfam01370    1 ILVTGATGFIGSHLVRRLLEKgYEVIGL---------DRLTSA-----------------SNTARLADLRFVEGDLTDRD 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   845 ALLcktdlyDVRNDGSISHLIHCAA--SVSFTQSLPAA-ATANISSPLYLqdLAASLAHEKTHFVHVSTAFVHGGLSGTD 921
Cdd:pfam01370   55 ALE------KLLADVRPDAVIHLAAvgGVGASIEDPEDfIEANVLGTLNL--LEAARKAGVKRFLFASSSEVYGDGAEIP 126

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 219113257   922 DEPLSErlfpLGSFDANDLYSsmqsteflASKAMRE 957
Cdd:pfam01370  127 QEETTL----TGPLAPNSPYA--------AAKLAGE 150
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
247-375 2.89e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.07  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   247 NVVVG---LAVRSLLDLYLlsrsFPEGSQIIICPPiNVPGMLRVLRHHRLEVVGVDLPPSDETtrnttttiSVDIEGIEA 323
Cdd:pfam00155   65 AVVFGsgaGANIEALIFLL----ANPGDAILVPAP-TYASYIRIARLAGGEVVRYPLYDSNDF--------HLDFDALEA 131

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 219113257   324 AITDKTVAILVVHPFGM--VSASNRDFERIKTLADQHKLDVMEDcaEIFTGLGS 375
Cdd:pfam00155  132 ALKEKPKVVLHTSPHNPtgTVATLEELEKLLDLAKEHNILLLVD--EAYAGFVF 183
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
764-993 6.26e-05

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 47.00  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  764 RKVILTGATGFIGSLVLRDLLlhRKVLGIKKVILicrskrgisaqariDTL-----LENtavygfLDKTEKSDLVKVIEG 838
Cdd:COG1088     2 MRILVTGGAGFIGSNFVRYLL--AKYPGAEVVVL--------------DKLtyagnLEN------LADLEDDPRYRFVKG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  839 DVTRPNALLcktdlyDVRNDGSISHLIHCAASVSFTQSL--PAA-------ATANIssplylqdLAASLAHEKTH--FVH 907
Cdd:COG1088    60 DIRDRELVD------ELFAEHGPDAVVHFAAESHVDRSIddPAAfvetnvvGTFNL--------LEAARKYWVEGfrFHH 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  908 VSTAFVHGGLSgtDDEPLSERlFPLgsfDANDLYSsmqsteflASKA-----MRelrfpnSY--TFskcvcehllvknsK 980
Cdd:COG1088   126 VSTDEVYGSLG--EDGPFTET-TPL---DPSSPYS--------ASKAasdhlVR------AYhrTY-------------G 172

                         250
                  ....*....|....
gi 219113257  981 VRTTIFRPS-IVGP 993
Cdd:COG1088   173 LPVVITRCSnNYGP 186
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 765-876 1.24e-04

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 45.72  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  765 KVILTGATGFIGSLVLRDLLLHrkvlgIKKVILICRSkrgisaQARIDTLLEntavygFLDKTEKSDLVKVIEGDvtrpn 844
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKA-----GYKVRGTVRS------LSKSAKLKA------LLKAAGYNDRLEFVIVD----- 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 219113257  845 aLLCKTDLYD--VRNdgsISHLIHCAASVSFTQS 876
Cdd:cd05227    59 -DLTAPNAWDeaLKG---VDYVIHVASPFPFTGP 88
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
769-915 1.56e-04

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 45.62  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257   769 TGATGFIGSLvLRDLLLHR--KVLGIKKvilicRSKRGisAQARIDTLLENTA------VYGflDKTEKSDLVKVIEgdV 840
Cdd:pfam16363    3 TGITGQDGSY-LAELLLEKgyEVHGIVR-----RSSSF--NTGRLEHLYDDHLngnlvlHYG--DLTDSSNLVRLLA--E 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219113257   841 TRPNAllcktdlydVRNDGSISHlihcaASVSFTQSLpAAATANISSPLYLQDLAASLAHE-KTHFVHVSTAFVHG 915
Cdd:pfam16363   71 VQPDE---------IYNLAAQSH-----VDVSFEQPE-YTADTNVLGTLRLLEAIRSLGLEkKVRFYQASTSEVYG 131
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 744-868 1.06e-03

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 43.14  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  744 RTSVFQSSPALRLPQCSPCERKVILTGATGFIGSLVLRdLLLHRkvlGIKKVILICRSKRGISAQARIDtLLENTAVYgf 823
Cdd:cd05274   131 RLVRAPAAALELAAAPGGLDGTYLITGGLGGLGLLVAR-WLAAR---GARHLVLLSRRGPAPRAAARAA-LLRAGGAR-- 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 219113257  824 ldkteksdlVKVIEGDVTRPNALlcKTDLYDVRNDGSISHLIHCA 868
Cdd:cd05274   204 ---------VSVVRCDVTDPAAL--AALLAELAAGGPLAGVIHAA 237
PRK02627 PRK02627
acetylornithine aminotransferase; Provisional
 317-417 1.39e-03

acetylornithine aminotransferase; Provisional


Pssm-ID: 235056 [Multi-domain]  Cd Length: 396  Bit Score: 42.81  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257  317 DIEGIEAAITDKTVAILV--------VHPfgmvsASNRDFERIKTLADQHKLDVMEDcaEIFTGLGslsyR-----GSPQ 383
Cdd:PRK02627  171 DIEALKAAITDKTAAVMLepiqgeggVNP-----ADKEYLQALRELCDENGILLILD--EVQTGMG----RtgklfAYQH 239

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 219113257  384 ADVVFVSFGLIKtstALGGGI---AMVKNIKVAETMK 417
Cdd:PRK02627  240 YGIEPDIMTLAK---GLGGGVpigAVLAKEKVADVFT 273
argD PRK03715
acetylornithine transaminase protein; Provisional
 317-374 1.94e-03

acetylornithine transaminase protein; Provisional


Pssm-ID: 179636 [Multi-domain]  Cd Length: 395  Bit Score: 42.37  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219113257  317 DIEGIEAAITDKTVAILV--VHPFGMVSASNRDF-ERIKTLADQHKLDVMEDcaEIFTGLG 374
Cdd:PRK03715  168 DIASVEKLITDKTVAVMLepVQGEGGVIPATREFmQQLRALTKQHGLLLIVD--EVQTGCG 226
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 1289-1455 3.04e-03

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 40.71  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1289 IGFLAKKVLRLCFNEVSVdlfsfaeaiREAENTGRPIRIVLTPTHRSVFDFILLsfLAFSLPELqvdIPFVAAAEDFRQl 1368
Cdd:cd07992     1 VRLLSRVILRIYFRRITV---------VGRENVPKDGPVIFLGNHPNALIDPLL--LAATLRRP---VRFLAKADLFKN- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219113257 1369 PIIGWLCSCARAIFIRR----GTGQVDPDSNQQI-----------QAIGIhrhgpvpvmevFIEGTrSRDGRFAKP-KTG 1432
Cdd:cd07992    66 PLIGWLLESFGAIPVYRpkdlARGGIGKISNAAVfdavgealkagGAIGI-----------FPEGG-SHDRPRLLPlKAG 133

                         170       180
                  ....*....|....*....|....*..
gi 219113257 1433 V---LKCLHQSG-IDSLIVPVAISYEA 1455
Cdd:cd07992   134 AarmALEALEAGqKDVKIVPVGLNYED 160
 
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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