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Conserved domains on  [gi|240120136|ref|NP_001155215|]
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3 beta-hydroxysteroid dehydrogenase/Delta 5--

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
5-357 2.10e-177

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 cd09811:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 354  Bit Score: 497.03  E-value: 2.10e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEKD-LEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 164 KAVLAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFILRGGGKFSTANP-VYVGNVAWAHILAARGLRN 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 243 PKKSpnIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCL-NSRWYLPVPILYWLAFLLETVSFLLSPIYRYIPPFNRHLVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLkTSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 240120136 322 LTASTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 2.10e-177

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 497.03  E-value: 2.10e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEKD-LEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 164 KAVLAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFILRGGGKFSTANP-VYVGNVAWAHILAARGLRN 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 243 PKKSpnIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCL-NSRWYLPVPILYWLAFLLETVSFLLSPIYRYIPPFNRHLVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLkTSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 240120136 322 LTASTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 1.12e-143

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 408.29  E-value: 1.12e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTsikVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNV---IKYIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   87 DVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  167 LAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFIL-RGGGKFSTANPVYVGNVAWAHILAARGLRNPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKfKTGDDNNLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240120136  246 SPNIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCLNSrWYLPV 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLPS-ISLPL 279
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-357 8.67e-48

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 164.00  E-value: 8.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKvfKPETREqffNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGH--EVVGLDR--SPPGAA---NLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 DVTGVIPRQTIlDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNsykdivlNGHEDEHRESTWSDPYPYSKKMAEKAV 166
Cdd:COG0451   76 GVGEEDPDETL-EVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDG-------EGPIDEDTPLRPVSPYGASKLAAELLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 167 LAANgsmlKNGGtLQTCALRPMCIYGER-SQFLSNTIIKALKNKFILRGGGKFSTANPVYVGNVAWAHILAARglrnpkk 245
Cdd:COG0451  148 RAYA----RRYG-LPVTILRPGNVYGPGdRGVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALE------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 246 SPNIQGEFYYISDDTPHqSYDDLNYTLSKEWGfclnsrwyLPVPILYwlaflletvsfllspiyryipPFNRHLVTLTAs 325
Cdd:COG0451  216 APAAPGGVYNVGGGEPV-TLRELAEAIAEALG--------RPPEIVY---------------------PARPGDVRPRR- 264
                        330       340       350
                 ....*....|....*....|....*....|..
gi 240120136 326 tftFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:COG0451  265 ---ADNSKARRELGWRPRTSLEEGLRETVAWY 293
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-170 2.33e-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: 61.28  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQ------------LLVQEKD----LEEIRVLDkvfkPETREQFFNLgTSIKVTVLEGDIL------ 64
Cdd:TIGR01746   3 LLTGATGFLGAYLLEellrrstrakviCLVRADSeehaMERLREAL----RSYRLWHENL-AMERIEVVAGDLSkprlgl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   65 -DTQYLRRAcQGISVVIHTAAIIDVtgVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpNSYKDIVLNGHE 143
Cdd:TIGR01746  78 sDAEWERLA-ENVDTIVHNGALVNH--VYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISV---GAAIDLSTGVTE 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 240120136  144 DEHRES---TWSDPYPYSKKMAEKAVLAAN 170
Cdd:TIGR01746 152 DDATVTpypGLAGGYTQSKWVAELLVREAS 181
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-268 3.38e-09

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 57.72  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAIID 87
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQAIEGCDAVFHTASPVF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  88 VTGVIPRQTILDVNLKGTQNLLEACIQ-ASVPAFIFSSSVDVA-------GPNSYKDIVLNGHEDEHRES-TWsdpYPYS 158
Cdd:PLN02986  90 FTVKDPQTELIDPALKGTINVLNTCKEtPSVKRVILTSSTAAVlfrqppiEANDVVDETFFSDPSLCRETkNW---YPLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 159 KKMAEKAVLaangSMLKNGGtLQTCALRPMCIYGERSQFLSNTIIKALKNkFIlrgGGKFSTANPVY----VGNVAWAHI 234
Cdd:PLN02986 167 KILAENAAW----EFAKDNG-IDMVVLNPGFICGPLLQPTLNFSVELIVD-FI---NGKNLFNNRFYrfvdVRDVALAHI 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 240120136 235 LAArglrnpkKSPNIQGEFYYisdDTPHQSYDDL 268
Cdd:PLN02986 238 KAL-------ETPSANGRYII---DGPIMSVNDI 261
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 1.05e-03

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 39.77  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136     7 LVTGAGGFLGQRIIQLLVQE--KDLeeirVL------DKVFKPETREQFFNLGTSikVTVLEGDILDTQYLRRACQGISV 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAERgaRRL----VLlsrsgpDAPGAAALLAELEAAGAR--VTVVACDVADRDALAAVLAAIPA 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240120136    79 -------VIHTAAIIDvTGVIPRQTILDVN------LKGTQNLLEACIQASVPAFIFSSSV 126
Cdd:smart00822  78 vegpltgVIHAAGVLD-DGVLASLTPERFAavlapkAAGAWNLHELTADLPLDFFVLFSSI 137
 
Name Accession Description Interval E-value
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-357 2.10e-177

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 497.03  E-value: 2.10e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEKD-LEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTA 83
Cdd:cd09811    1 VCLVTGGGGFLGQHIIRLLLERKEeLKEIRVLDKAFGPELIEHFEKSQGKTYVTDIEGDIKDLSFLFRACQGVSVVIHTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAE 163
Cdd:cd09811   81 AIVDVFGPPNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFKGRPIFNGVEDTPYEDTSTPPYASSKLLAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 164 KAVLAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFILRGGGKFSTANP-VYVGNVAWAHILAARGLRN 242
Cdd:cd09811  161 NIVLNANGAPLKQGGYLVTCALRPMYIYGEGSHFLTEIFDFLLTNNGWLFPRIKGSGVNPlVYVGNVAWAHILAAKALQV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 243 PKKSpnIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCL-NSRWYLPVPILYWLAFLLETVSFLLSPIYRYIPPFNRHLVT 321
Cdd:cd09811  241 PDKA--IRGQFYFISDDTPHNSYSDFNYELLKELGLRLkTSWWYVPLFLLYFLAFLLEIVSFLLRPYVKYRPRYNRHAVA 318
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 240120136 322 LTASTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09811  319 LTNSMFTFSYLKAQRHFGYMPLFSWEESKERTAKWV 354
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
7-288 1.12e-143

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 408.29  E-value: 1.12e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTsikVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGELKEVRVFDLRESPELLEDFSKSNV---IKYIQGDVTDKDDLDNALEGVDVVIHTASAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   87 DVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHRESTWSDPYPYSKKMAEKAV 166
Cdd:pfam01073  78 DVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPILNGDEETPYESTHQDAYPRSKAIAEKLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  167 LAANGSMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNKFIL-RGGGKFSTANPVYVGNVAWAHILAARGLRNPKK 245
Cdd:pfam01073 158 LKANGRPLKNGGRLYTCALRPAGIYGEGDRLLVPFIVNLAKLGLAKfKTGDDNNLSDRVYVGNVAWAHILAARALQDPKK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240120136  246 SPNIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCLNSrWYLPV 288
Cdd:pfam01073 238 MSSIAGNAYFIYDDTPVQSYDDFNRTLLKSLGYDLPS-ISLPL 279
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
5-357 3.00e-110

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 325.54  E-value: 3.00e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEkDLEEIRVLDKVFKPETREQFFNlgTSIKVtvLEGDILDTQYLRRACQGISVVIHTAA 84
Cdd:cd05241    1 SVLVTGGSGFFGERLVKQLLER-GGTYVRSFDIAPPGEALSAWQH--PNIEF--LKGDITDRNDVEQALSGADCVFHTAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGviPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPnsyKDIVLNGHEDEHRESTWSDPYPYSKKMAEK 164
Cdd:cd05241   76 IVPLAG--PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFG---GQNIHNGDETLPYPPLDSDMYAETKAIAEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 165 AVLAANGSmlkngGTLQTCALRPMCIYGERSQFLSNTIIKALKNK-FILRGGGKFSTANPVYVGNVAWAHILAARGLRNP 243
Cdd:cd05241  151 IVLEANGR-----DDLLTCALRPAGIFGPGDQGLVPILFEWAEKGlVKFVFGRGNNLVDFTYVHNLAHAHILAAAALVKG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 244 KKspnIQGEFYYISDDTPHQSYDDLNYTLsKEWGFCLNSRWYLPVPILYWLAFLLETVSFLLSPIYRYIPPFNRHLVTlt 323
Cdd:cd05241  226 KT---ISGQTYFITDAEPHNMFELLRPVW-KALGFGSRPKIRLSGPLAYCAALLSELVSFMLGPYFVFSPFYVRALVT-- 299
                        330       340       350
                 ....*....|....*....|....*....|....
gi 240120136 324 asTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd05241  300 --PMYFSIAKAQKDLGYAPRYSNEEGLIETLNWY 331
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
5-357 1.51e-65

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. 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 sythase 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: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 211.06  E-value: 1.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVqEKDLEEIRVLDkvfkpeTREQFFNLGTSIK-VTVLEGDILDTQYLRRA--CQGISVVIH 81
Cdd:cd09813    1 SCLVVGGSGFLGRHLVEQLL-RRGNPTVHVFD------IRPTFELDPSSSGrVQFHTGDLTDPQDLEKAfnEKGPNVVFH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  82 TAAIIDVTGvipRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAgpnSYKDIVLNGHEDEHRESTWSDPYPYSKKM 161
Cdd:cd09813   74 TASPDHGSN---DDLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVV---FNGQDIINGDESLPYPDKHQDAYNETKAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 162 AEKAVLAANGSMLKnggtLQTCALRPMCIYGERSQFLSNTIIKALKN---KFILrGGGK----FStanpvYVGNVAWAHI 234
Cdd:cd09813  148 AEKLVLKANDPESG----LLTCALRPAGIFGPGDRQLVPGLLKAAKNgktKFQI-GDGNnlfdFT-----YVENVAHAHI 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 235 LAARGLRNPKKSPNIQGEFYYISDDTPHQSYDdLNYTLSKEWGFCLNSRWYLPVPILYWLAFLLETVSFLLSPIyryiPP 314
Cdd:cd09813  218 LAADALLSSSHAETVAGEAFFITNDEPIYFWD-FARAIWEGLGYERPPSIKLPRPVALYLASLLEWTCKVLGKE----PT 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 240120136 315 FNRHLVTLTASTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd09813  293 FTPFRVALLCSTRYFNIEKAKKRLGYTPVVTLEEGIERTLQWF 335
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
5-342 2.08e-49

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. 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 sythase 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: 187672 [Multi-domain]  Cd Length: 339  Bit Score: 169.22  E-value: 2.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEKD---LEEIRVLDKVFKPETReqffnlgtsikvtVLEGDILDTQYLRRACQGISVVIH 81
Cdd:cd09812    1 SVLITGGGGYFGFRLGCALAKSGVhviLFDIRRPQQELPEGIK-------------FIQADVRDLSQLEKAVAGVDCVFH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  82 TAAIiDVTGV--IPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVA-GPNSYKdivlNGHE-------DEHrestw 151
Cdd:cd09812   68 IASY-GMSGReqLNRELIEEINVRGTENIIQVCVRRRVPRLIYTSTFNVIfGGQPIR----NGDEslpylplDLH----- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 152 SDPYPYSKKMAEKAVLAANGSMLKN-GGTLQTCALRPMCIYGERSQFLSNTIIKALKNK-FILRGGGKFSTANPVYVGNV 229
Cdd:cd09812  138 VDHYSRTKSIAEQLVLKANNMPLPNnGGVLRTCALRPAGIYGPGEQRHLPRIVSYIEKGlFMFVYGDPKSLVEFVHVDNL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 230 AWAHILAARGLRNPKKSpNIQGEFYYISDDTPHQSYDDLNyTLSKEWGFCLNSrWYLPVPILYWLAFLLETVSFLLSPIY 309
Cdd:cd09812  218 VQAHILAAEALTTAKGY-IASGQAYFISDGRPVNNFEFFR-PLVEGLGYSFPS-LRLPLSLVYFFAFLTEMVHFALGPIC 294
                        330       340       350
                 ....*....|....*....|....*....|...
gi 240120136 310 RYIPPFNRHLVTLTASTFTFSYKKAQRDLGYEP 342
Cdd:cd09812  295 NFQPLLTRTEVYKTGVTHYFSIEKARAELGYEP 327
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-357 8.67e-48

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 164.00  E-value: 8.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKvfKPETREqffNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGH--EVVGLDR--SPPGAA---NLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 DVTGVIPRQTIlDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNsykdivlNGHEDEHRESTWSDPYPYSKKMAEKAV 166
Cdd:COG0451   76 GVGEEDPDETL-EVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDG-------EGPIDEDTPLRPVSPYGASKLAAELLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 167 LAANgsmlKNGGtLQTCALRPMCIYGER-SQFLSNTIIKALKNKFILRGGGKFSTANPVYVGNVAWAHILAARglrnpkk 245
Cdd:COG0451  148 RAYA----RRYG-LPVTILRPGNVYGPGdRGVLPRLIRRALAGEPVPVFGDGDQRRDFIHVDDVARAIVLALE------- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 246 SPNIQGEFYYISDDTPHqSYDDLNYTLSKEWGfclnsrwyLPVPILYwlaflletvsfllspiyryipPFNRHLVTLTAs 325
Cdd:COG0451  216 APAAPGGVYNVGGGEPV-TLRELAEAIAEALG--------RPPEIVY---------------------PARPGDVRPRR- 264
                        330       340       350
                 ....*....|....*....|....*....|..
gi 240120136 326 tftFSYKKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:COG0451  265 ---ADNSKARRELGWRPRTSLEEGLRETVAWY 293
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
7-357 6.31e-43

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. 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. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. 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: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 151.67  E-value: 6.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLdkvfkpeTREQ-----FFNLGtsikVTVLEGDILDTQYLRRACQGISVVIH 81
Cdd:cd05228    2 LVTGATGFLGSNLVRALLAQG--YRVRAL-------VRSGsdavlLDGLP----VEVVEGDLTDAASLAAAMKGCDRVFH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  82 TAAIIDVTGVIPRQtILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSykdivlNGHEDEH---RESTWSDPYPYS 158
Cdd:cd05228   69 LAAFTSLWAKDRKE-LYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPP------DGRIDETtpwNERPFPNDYYRS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 159 KKMAEKAVLAAngsmLKNGgtLQTCALRPMCIYGERSqfLSNT-----IIKALKNK--FILRGGGKFstanpVYVGNVAW 231
Cdd:cd05228  142 KLLAELEVLEA----AAEG--LDVVIVNPSAVFGPGD--EGPTstgldVLDYLNGKlpAYPPGGTSF-----VDVRDVAE 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 232 AHILAA-RGLRnpkkspniqGEFYYISDdtPHQSYDDLNYTLSKEWGfclnsRWYLPVPILYWLAFLLETVSFLLSPIYR 310
Cdd:cd05228  209 GHIAAMeKGRR---------GERYILGG--ENLSFKQLFETLAEITG-----VKPPRRTIPPWLLKAVAALSELKARLTG 272
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 240120136 311 YIPPFNRHLVTLTASTFTFSYKKAQRDLGYEPlVSWEEAKQKTSEWI 357
Cdd:cd05228  273 KPPLLTPRTARVLRRNYLYSSDKARRELGYSP-RPLEEALRDTLAWL 318
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
7-249 1.81e-26

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: 105.46  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDKvfkpetREQFFNLGTSIKVTVLEGDILDTQYLRRACQ--GISVVIHTAA 84
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKG--YEVIGLDR------LTSASNTARLADLRFVEGDLTDRDALEKLLAdvRPDAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   85 I--IDVTGVIPRQTIlDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPnsykdivlnGHEDEHRESTWSD------PYP 156
Cdd:pfam01370  74 VggVGASIEDPEDFI-EANVLGTLNLLEAARKAGVKRFLFASSSEVYGD---------GAEIPQEETTLTGplapnsPYA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  157 YSKKMAEKAVLAANGSmlkngGTLQTCALRPMCIYGER------SQFLSNTIIKALKNK-FILRGGGK----FstanpVY 225
Cdd:pfam01370 144 AAKLAGEWLVLAYAAA-----YGLRAVILRLFNVYGPGdnegfvSRVIPALIRRILEGKpILLWGDGTqrrdF-----LY 213
                         250       260
                  ....*....|....*....|....
gi 240120136  226 VGNVAWAHILAargLRNPKKSPNI 249
Cdd:pfam01370 214 VDDVARAILLA---LEHGAVKGEI 234
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
6-357 2.52e-25

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 104.22  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   6 CLVTGAGGFLGQRIIQLLVqeKDLEEIRVLDK--VFKPETREQFfnlgtSIKVTVLEGDILDTQYLRRACQGISVVIHTA 83
Cdd:cd05256    2 VLVTGGAGFIGSHLVERLL--ERGHEVIVLDNlsTGKKENLPEV-----KPNVKFIEGDIRDDELVEFAFEGVDYVFHQA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIIDVTGVI--PRQTiLDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIvlngheDEHRESTWSDPYPYSKKM 161
Cdd:cd05256   75 AQASVPRSIedPIKD-HEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPK------DEDHPPNPLSPYAVSKYA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 162 AEKAVLAANGSMlknggTLQTCALRPMCIYGERSQ-------FLSNTIIKALKNK-FILRGGGKfSTANPVYVGNVAWAH 233
Cdd:cd05256  148 GELYCQVFARLY-----GLPTVSLRYFNVYGPRQDpnggyaaVIPIFIERALKGEpPTIYGDGE-QTRDFTYVEDVVEAN 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 234 ILAARglrnpKKSPniqGEFYYISDDTPHQsyddLNYtlskewgfclnsrwylpvpilywLAFLL-ETVSFLLSPIyrYI 312
Cdd:cd05256  222 LLAAT-----AGAG---GEVYNIGTGKRTS----VNE-----------------------LAELIrEILGKELEPV--YA 264
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 240120136 313 PPF---NRHlvTLTASTftfsykKAQRDLGYEPLVSWEEAKQKTSEWI 357
Cdd:cd05256  265 PPRpgdVRH--SLADIS------KAKKLLGWEPKVSFEEGLRLTVEWF 304
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
6-250 2.77e-23

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: 95.83  E-value: 2.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   6 CLVTGAGGFLGQRIIQLLVQEKDleeirvldkvfkpetreqffnlgtsiKVTVLegDILDtqylrracqgisVVIHTAAI 85
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGH--------------------------EVVVI--DRLD------------VVVHLAAL 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  86 IDVTGVIPRQT-ILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIvlnghEDEHRESTwSDPYPYSKKMAEK 164
Cdd:cd08946   41 VGVPASWDNPDeDFETNVVGTLNLLEAARKAGVKRFVYASSASVYGSPEGLPE-----EEETPPRP-LSPYGVSKLAAEH 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 165 AVLAANgsmlkNGGTLQTCALRPMCIYGER-----SQFLSNTIIKALKNKFI-LRGGGKFsTANPVYVGNVAWAHILAAR 238
Cdd:cd08946  115 LLRSYG-----ESYGLPVVILRLANVYGPGqrprlDGVVNDFIRRALEGKPLtVFGGGNQ-TRDFIHVDDVVRAILHALE 188
                        250
                 ....*....|..
gi 240120136 239 GLRNPKKSPNIQ 250
Cdd:cd08946  189 NPLEGGGVYNIG 200
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-353 3.80e-20

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 89.72  E-value: 3.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLdkvfkpeTReqffnLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:cd05232    3 LVTGANGFIGRALVDKLLSRG--EEVRIA-------VR-----NAENAEPSVVLAELPDIDSFTDLFLGVDAVVHLAARV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 DV---TGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSykdivLNGHEDEHRESTWSDPYPYSKKMAE 163
Cdd:cd05232   69 HVmndQGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEGT-----VGAPFDETDPPAPQDAYGRSKLEAE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 164 KAV--LAANGSMlknggtlQTCALRPMCIYGE--RSQFLSntIIKALKNKFILRGGGKFSTANPVYVGNVAWAHILAarg 239
Cdd:cd05232  144 RALleLGASDGM-------EVVILRPPMVYGPgvRGNFAR--LMRLIDRGLPLPPGAVKNRRSLVSLDNLVDAIYLC--- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 240 LRNPKKSpniqGEFYYISDDTP---HQSYDDLNYTLSKewgfclnSRWYLPVPilywlAFLLETVSFLL---SPIYRyip 313
Cdd:cd05232  212 ISLPKAA----NGTFLVSDGPPvstAELVDEIRRALGK-------PTRLLPVP-----AGLLRFAAKLLgkrAVIQR--- 272
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 240120136 314 pfnrhlvtLTAStFTFSYKKAQRDLGYEPLVSWEEAKQKT 353
Cdd:cd05232  273 --------LFGS-LQYDPEKTQNELGWRPPISLEEGLQET 303
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
7-243 5.14e-20

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 87.21  E-value: 5.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLdkVFKPETREQFFNLGtsikVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARG--HPVRAL--VRDPEKAAALAAAG----VEVVQGDLDDPESLAAALAGVDAVFLLVPSG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 DVTGViprqtilDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNsykdivLNGHEDEHREstwsdpypyskkmAEKAV 166
Cdd:COG0702   75 PGGDF-------AVDVEGARNLADAAKAAGVKRIVYLSALGADRDS------PSPYLRAKAA-------------VEEAL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 167 LAANgsmlknggtLQTCALRPmciygerSQFLSN--TIIKALKNKFILR---GGGKFStanPVYVGNVAWAhilAARGLR 241
Cdd:COG0702  129 RASG---------LPYTILRP-------GWFMGNllGFFERLRERGVLPlpaGDGRVQ---PIAVRDVAEA---AAAALT 186

                 ..
gi 240120136 242 NP 243
Cdd:COG0702  187 DP 188
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
7-169 6.03e-20

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: 88.34  E-value: 6.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQ-----------LLVQEKDLEEIRV-LDKVFKpetreqFFNLGTSI---KVTVLEGDI------LD 65
Cdd:COG3320    4 LLTGATGFLGAHLLRellrrtdarvyCLVRASDEAAARErLEALLE------RYGLWLELdasRVVVVAGDLtqprlgLS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  66 TQYLRRACQGISVVIHTAAIIDVTGviPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLnghEDE 145
Cdd:COG3320   78 EAEFQELAEEVDAIVHLAALVNLVA--PYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFE---EDD 152
                        170       180
                 ....*....|....*....|....*
gi 240120136 146 HRE-STWSDPYPYSKKMAEKAVLAA 169
Cdd:COG3320  153 LDEgQGFANGYEQSKWVAEKLVREA 177
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
6-236 7.15e-20

flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. 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: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 88.79  E-value: 7.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   6 CLVTGAGGFLGQRIIQLLVQE--------KDLEEIRVLDKVFKPEtreqffnlGTSIKVTVLEGDILDTQYLRRACQGIS 77
Cdd:cd08958    1 VCVTGASGFIGSWLVKRLLQRgytvratvRDPGDEKKVAHLLELE--------GAKERLKLFKADLLDYGSFDAAIDGCD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  78 VVIHTAAIIDVTGVIPRQTILDVNLKGTQNLLEACIQA-SVPAFIFSSSVD--VAGPNSYKDIVLNghedehrESTWSDP 154
Cdd:cd08958   73 GVFHVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKAkSVKRVVFTSSVAavVWNPNRGEGKVVD-------ESCWSDL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 155 ---------YPYSKKMAEKAVLA-ANGSMLK----NGGTLQTCALRPmciygeRSQFLSNTIIKALKNKFILRGGGKFST 220
Cdd:cd08958  146 dfckktklwYALSKTLAEKAAWEfAEENGLDlvtvNPSLVVGPFLQP------SLNSSSQLILSLLKGNAEMYQNGSLAL 219
                        250
                 ....*....|....*.
gi 240120136 221 anpVYVGNVAWAHILA 236
Cdd:cd08958  220 ---VHVDDVADAHILL 232
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
6-193 1.44e-19

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: 87.81  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   6 CLVTGAGGFLGQRIIQLLVQEKdlEEIRVLDKVFKPETREQFFNLG--TSIKVTVLEGDI------LDTQYLRRACQGIS 77
Cdd:cd05263    1 VFVTGGTGFLGRHLVKRLLENG--FKVLVLVRSESLGEAHERIEEAglEADRVRVLEGDLtqpnlgLSAAASRELAGKVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  78 VVIHTAAIIDVTgvIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSykDIVlNGHEDEHREsTWSDPYPY 157
Cdd:cd05263   79 HVIHCAASYDFQ--APNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNRE--GNI-RETELNPGQ-NFKNPYEQ 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 240120136 158 SKKMAEKAVLAAngsmlknGGTLQTCALRPMCIYGE 193
Cdd:cd05263  153 SKAEAEQLVRAA-------ATQIPLTVYRPSIVVGD 181
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
6-317 4.24e-19

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 86.15  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   6 CLVTGAGGFLGQRIIQLLVqeKDLEEIRVLDKVFKPETREQFFNLGTSIkvTVLEGDILDTQYLRRACQGISVVIHTAAI 85
Cdd:cd05271    3 VTVFGATGFIGRYVVNRLA--KRGSQVIVPYRCEAYARRLLVMGDLGQV--LFVEFDLRDDESIRKALEGSDVVINLVGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  86 IDVTGvipRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpnsykdivlngheDEHREStwsdPYPYSKKMAEKA 165
Cdd:cd05271   79 LYETK---NFSFEDVHVEGPERLAKAAKEAGVERLIHISALGA---------------DANSPS----KYLRSKAEGEEA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 166 VLAAngsmlknggtLQTCA-LRPMCIYGERSQFLSNTIIKALKNKFILRGGGKFSTANPVYVGNVAWAhilAARGLRNpk 244
Cdd:cd05271  137 VREA----------FPEATiVRPSVVFGREDRFLNRFAKLLAFLPFPPLIGGGQTKFQPVYVGDVAEA---IARALKD-- 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240120136 245 ksPNIQGEFYYISDdtPHQsyddlnYTLSK--EWGFCLNSRWYLPVPILYWLAFLLETVSFLLSPIYryiPPFNR 317
Cdd:cd05271  202 --PETEGKTYELVG--PKV------YTLAElvELLRRLGGRKRRVLPLPLWLARLIARVKLLLLLPE---PPLTR 263
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
7-165 1.69e-18

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: 85.01  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQE--------KDLEEIRVLDKVFKPETREQffnlgtSIKVTVLEgDILDTQYLRRACQGISV 78
Cdd:cd05227    3 LVTGATGFIASHIVEQLLKAgykvrgtvRSLSKSAKLKALLKAAGYND------RLEFVIVD-DLTAPNAWDEALKGVDY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  79 VIHTAAIIDVTGVIPRQTILDVNLKGTQNLLEACIQA-SVPAFIF-SSSVDVAGPNSY-KDIVLNghEDEHRESTWS--- 152
Cdd:cd05227   76 VIHVASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKAAgSVKRVVLtSSVAAVGDPTAEdPGKVFT--EEDWNDLTISksn 153
                        170
                 ....*....|....*
gi 240120136 153 --DPYPYSKKMAEKA 165
Cdd:cd05227  154 glDAYIASKTLAEKA 168
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
7-163 1.89e-17

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. 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: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 82.05  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVfKPETReqffnlGTSIKVTVLEGDiLDTQYLRRA--CQGISVVIHTAA 84
Cdd:cd05238    4 LITGASGFVGQRLAERLLSDVPNERLILIDVV-SPKAP------SGAPRVTQIAGD-LAVPALIEAlaNGRPDVVFHLAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGVIPRQTILDVNLKGTQNLLEAC-IQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDehreSTWSdpYPYSKKMAE 163
Cdd:cd05238   76 IVSGGAEADFDLGYRVNVDGTRNLLEALrKNGPKPRFVFTSSLAVYGLPLPNPVTDHTALD----PASS--YGAQKAMCE 149
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
7-174 2.77e-15

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: 75.38  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEK------------DLEEIRV-LDKVFKpETREQFFNLGTSIKVTVLEGDI------LDTQ 67
Cdd:cd05235    3 LLTGATGFLGAYLLRELLKRKnvskiyclvrakDEEAALErLIDNLK-EYGLNLWDELELSRIKVVVGDLskpnlgLSDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  68 YLRRACQGISVVIHTAAiiDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLNGHEDEHR 147
Cdd:cd05235   82 DYQELAEEVDVIIHNGA--NVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEESDDMLE 159
                        170       180
                 ....*....|....*....|....*...
gi 240120136 148 EST-WSDPYPYSKKMAEKAVLAANGSML 174
Cdd:cd05235  160 SQNgLPNGYIQSKWVAEKLLREAANRGL 187
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
7-192 1.01e-14

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. 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: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 73.94  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVfKPETREQffnlgtsiKVTVLEGDILDTQ---YLRRAcqGISVVIHTA 83
Cdd:cd05240    2 LVTGAAGGLGRLLARRLAASPRVIGVDGLDRR-RPPGSPP--------KVEYVRLDIRDPAaadVFRER--EADAVVHLA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIID--VTGVIPRQtildVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIVLngHEDEHRESTWSDPYPYSKKM 161
Cdd:cd05240   71 FILDppRDGAERHR----INVDGTQNVLDACAAAGVPRVVVTSSVAVYGAHPDNPAPL--TEDAPLRGSPEFAYSRDKAE 144
                        170       180       190
                 ....*....|....*....|....*....|.
gi 240120136 162 AEKAVLAAngsmLKNGGTLQTCALRPMCIYG 192
Cdd:cd05240  145 VEQLLAEF----RRRHPELNVTVLRPATILG 171
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
7-215 3.16e-14

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. 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: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 72.72  E-value: 3.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLD------KVFKPETREQffnlgtsIKVTVLEGDILDTQYLRRACQGISVVI 80
Cdd:cd05257    3 LVTGADGFIGSHLTERLLREG--HEVRALDiynsfnSWGLLDNAVH-------DRFHFISGDVRDASEVEYLVKKCDVVF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  81 HTAAIIDV-TGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIvlngHED--EHRESTWSDPYPY 157
Cdd:cd05257   74 HLAALIAIpYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPI----DEDhpLLYINKPRSPYSA 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240120136 158 SKKMAEKAVLAangSMLKNGgtLQTCALRPMCIYGERSQFLS--NTIIKA-LKNKFILRGG 215
Cdd:cd05257  150 SKQGADRLAYS---YGRSFG--LPVTIIRPFNTYGPRQSARAviPTIISQrAIGQRLINLG 205
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
7-208 5.59e-14

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: 69.35  E-value: 5.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKvfkpetREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAii 86
Cdd:cd05226    2 LILGATGFIGRALARELLEQGH--EVTLLVR------NTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAG-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 dvtGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpnsYKDIVLNGHEDEhrestwSDPYPYSKKMAEKAV 166
Cdd:cd05226   72 ---APRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGA-----YGDLHEETEPSP------SSPYLAVKAKTEAVL 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 240120136 167 LAANgsmlknggtLQTCALRPMCIYGErsqfLSNTIIKALKN 208
Cdd:cd05226  138 REAS---------LPYTIVRPGVIYGD----LARAIANAVVT 166
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
7-136 1.11e-13

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 69.19  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLdkVFKPETREQFFNLGtsikVTVLEGDILDTQYLRRACQGISVVIHTAAIi 86
Cdd:cd05243    3 LVVGATGKVGRHVVRELLDRG--YQVRAL--VRDPSQAEKLEAAG----AEVVVGDLTDAESLAAALEGIDAVISAAGS- 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 dvtGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKD 136
Cdd:cd05243   74 ---GGKGGPRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLE 120
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-164 1.15e-13

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 71.03  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDkvfkpetreqffNLGTS----------IKVTVLEGDILDTQYLRR--ACQ 74
Cdd:cd05247    3 LVTGGAGYIGSHTVVELLEAG--YDVVVLD------------NLSNGhrealpriekIRIEFYEGDIRDRAALDKvfAEH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  75 GISVVIHTAAIIDVtGVIPRQTIL--DVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKDIvlnghEDEHRESTwS 152
Cdd:cd05247   69 KIDAVIHFAALKAV-GESVQKPLKyyDNNVVGTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVPI-----TEEAPLNP-T 141
                        170
                 ....*....|..
gi 240120136 153 DPYPYSKKMAEK 164
Cdd:cd05247  142 NPYGRTKLMVEQ 153
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
8-193 1.30e-13

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: 69.95  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    8 VTGAGGFLGQRIIQ-------------LLVQEKDLEEI--RVLDKVFKPETREQFFNLGTSiKVTVLEGDI------LDT 66
Cdd:pfam07993   1 LTGATGFLGKVLLEkllrstpdvkkiyLLVRAKDGESAleRLRQELEKYPLFDALLKEALE-RIVPVAGDLsepnlgLSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   67 QYLRRACQGISVVIHTAAIIDVTGviPRQTILDVNLKGTQNLLEACIQ-ASVPAFIFSSSvDVAGPNSYKDI---VLNGH 142
Cdd:pfam07993  80 EDFQELAEEVDVIIHSAATVNFVE--PYDDARAVNVLGTREVLRLAKQgKQLKPFHHVST-AYVNGERGGLVeekPYPEG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240120136  143 EDEHREST--------WSDPYPYSKKMAEKAVLAAngsmlkNGGTLQTCALRPMCIYGE 193
Cdd:pfam07993 157 EDDMLLDEdepallggLPNGYTQTKWLAEQLVREA------ARRGLPVVIYRPSIITGE 209
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
7-170 1.71e-12

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 67.15  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRII-QLLvqEKDLEEIRVLD----KVF--KPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQ--GIS 77
Cdd:pfam02719   2 LVTGGGGSIGSELCrQIL--KFNPKKIILFSrdelKLYeiRQELREKFNDPKLRFFIVPVIGDVRDRERLERAMEqyGVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   78 VVIHTAAIIDVTGV--IPRQTILdVNLKGTQNLLEACIQASVPAFIFSSSVDVAGP-NSYkdivlnGHedehrestwsdp 154
Cdd:pfam02719  80 VVFHAAAYKHVPLVeyNPMEAIK-TNVLGTENVADAAIEAGVKKFVLISTDKAVNPtNVM------GA------------ 140
                         170
                  ....*....|....*.
gi 240120136  155 ypySKKMAEKAVLAAN 170
Cdd:pfam02719 141 ---TKRLAEKLFQAAN 153
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
7-125 1.79e-12

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 67.35  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDkvfkpetreqffNLGTS------IKVTVLEGDILDTQYLRRACQ--GISV 78
Cdd:COG1087    4 LVTGGAGYIGSHTVVALLEAG--HEVVVLD------------NLSNGhreavpKGVPFVEGDLRDRAALDRVFAehDIDA 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 240120136  79 VIHTAAIIDVtG---VIPRQTiLDVNLKGTQNLLEACIQASVPAFIFSSS 125
Cdd:COG1087   70 VIHFAALKAV-GesvEKPLKY-YRNNVVGTLNLLEAMREAGVKRFVFSSS 117
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
7-172 7.03e-12

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. 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: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 65.33  E-value: 7.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEkDLEEIRVLD----KVFkpETREQFFNLGTSIKVTVLEGDILDTQYLRRAC--QGISVVI 80
Cdd:cd05237    6 LVTGGAGSIGSELVRQILKF-GPKKLIVFDrdenKLH--ELVRELRSRFPHDKLRFIIGDVRDKERLRRAFkeRGPDIVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  81 HTAAIIDVTGV--IPRQTIlDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGP-NSYkdivlnGHedehrestwsdpypy 157
Cdd:cd05237   83 HAAALKHVPSMedNPEEAI-KTNVLGTKNVIDAAIENGVEKFVCISTDKAVNPvNVM------GA--------------- 140
                        170
                 ....*....|....*
gi 240120136 158 SKKMAEKAVLAANGS 172
Cdd:cd05237  141 TKRVAEKLLLAKNEY 155
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
7-192 1.22e-11

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: 65.01  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQ-LLVQEKDLEEIRVL---DKVFKPETR-------------EQFFNLGTSiKVTVLEGDI------ 63
Cdd:cd05236    4 LITGATGFLGKVLLEkLLRSCPDIGKIYLLirgKSGQSAEERlrellkdklfdrgRNLNPLFES-KIVPIEGDLsepnlg 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  64 LDTQYLRRACQGISVVIHTAAIIDVTGVIPrqTILDVNLKGTQNLLEACIQ-ASVPAFIFSSSVDVAGPNSY-------- 134
Cdd:cd05236   83 LSDEDLQTLIEEVNIIIHCAATVTFDERLD--EALSINVLGTLRLLELAKRcKKLKAFVHVSTAYVNGDRQLieekvypp 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240120136 135 --------KDIVLNghEDEHREST-------WSDPYPYSKKMAEKAVlaangsmLKNGGTLQTCALRPMCIYG 192
Cdd:cd05236  161 padpekliDILELM--DDLELERAtpkllggHPNTYTFTKALAERLV-------LKERGNLPLVIVRPSIVGA 224
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
7-356 3.66e-11

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: 63.34  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQ--GISVVIHTAA 84
Cdd:cd05246    4 LVTGGAGFIGSNFVRYLLNKYPDYKIINLDKLTYAGNLENLEDVSSSPRYRFVKGDICDAELVDRLFEeeKIDAVIHFAA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGVI--PRQTIlDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpnsYKDIVLNGHEDEHRESTWSDPYPYSKKMA 162
Cdd:cd05246   84 ESHVDRSIsdPEPFI-RTNVLGTYTLLEAARKYGVKRFVHISTDEV-----YGDLLDDGEFTETSPLAPTSPYSASKAAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 163 EKAVLAANGSmlkngGTLQTCALRPMCIYGERsQF----LSNTIIKALKNKFI-LRGGGKfSTANPVYVGNVAWA-HILA 236
Cdd:cd05246  158 DLLVRAYHRT-----YGLPVVITRCSNNYGPY-QFpeklIPLFILNALDGKPLpIYGDGL-NVRDWLYVEDHARAiELVL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 237 ARGlrnpkkspnIQGEFYYISDdtpHQSYDDLNytlskewgfclnsrwylpvpilywlafLLETVSFLLS---PIYRYIP 313
Cdd:cd05246  231 EKG---------RVGEIYNIGG---GNELTNLE---------------------------LVKLILELLGkdeSLITYVK 271
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 240120136 314 --PFNRHLVTLTAStftfsykKAQRDLGYEPLVSWEEAKQKTSEW 356
Cdd:cd05246  272 drPGHDRRYAIDSS-------KIRRELGWRPKVSFEEGLRKTVRW 309
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
7-170 2.33e-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: 61.28  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQ------------LLVQEKD----LEEIRVLDkvfkPETREQFFNLgTSIKVTVLEGDIL------ 64
Cdd:TIGR01746   3 LLTGATGFLGAYLLEellrrstrakviCLVRADSeehaMERLREAL----RSYRLWHENL-AMERIEVVAGDLSkprlgl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   65 -DTQYLRRAcQGISVVIHTAAIIDVtgVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpNSYKDIVLNGHE 143
Cdd:TIGR01746  78 sDAEWERLA-ENVDTIVHNGALVNH--VYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISV---GAAIDLSTGVTE 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 240120136  144 DEHRES---TWSDPYPYSKKMAEKAVLAAN 170
Cdd:TIGR01746 152 DDATVTpypGLAGGYTQSKWVAELLVREAS 181
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
7-356 1.60e-09

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended 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: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 58.50  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleeiRVL---------DKVFKPETREQffnLGTSIKVTVLEGDILDTQYLRRACQ--G 75
Cdd:cd05253    4 LVTGAAGFIGFHVAKRLLERGD----EVVgidnlndyyDVRLKEARLEL---LGKSGGFKFVKGDLEDREALRRLFKdhE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  76 ISVVIHTAAIIDVTGVI--PRqTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAG-----PNSYKDIVlnghedEHRE 148
Cdd:cd05253   77 FDAVIHLAAQAGVRYSLenPH-AYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYGlntkmPFSEDDRV------DHPI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 149 StwsdPYPYSKKMAEkaVLAANGSMLKNggtLQTCALRPMCIYGE-----RSQFLsntIIKALKNkfilrggGK----FS 219
Cdd:cd05253  150 S----LYAATKKANE--LMAHTYSHLYG---IPTTGLRFFTVYGPwgrpdMALFL---FTKAILE-------GKpidvFN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 220 TANP----VYVGNVAWAHILAArglrNPKKSPNIQGEFYYISDDTPHQSYDDLNYTlskewgfclNSRwylPVPILYWLA 295
Cdd:cd05253  211 DGNMsrdfTYIDDIVEGVVRAL----DTPAKPNPNWDAEAPDPSTSSAPYRVYNIG---------NNS---PVKLMDFIE 274
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240120136 296 fLLEtvSFLLSPIYRYIPPFNRHLVTLT-ASTftfsyKKAQRDLGYEPLVSWEEAKQKTSEW 356
Cdd:cd05253  275 -ALE--KALGKKAKKNYLPMQKGDVPETyADI-----SKLQRLLGYKPKTSLEEGVKRFVEW 328
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
7-209 1.72e-09

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. 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: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 58.46  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVqeKDLEEIRVLDKVfkpeTREQFFNLGTSIK-------VTVLEGDILDTQYLRRACQGISVV 79
Cdd:cd05258    4 LITGGAGFIGSNLARFFL--KQGWEVIGFDNL----MRRGSFGNLAWLKanredggVRFVHGDIRNRNDLEDLFEDIDLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  80 IHTAAIIDVTGVI--PRQTIlDVNLKGTQNLLEACIQASVPA-FIFSSSVDVAG--PNSykdivLNGHEDEHR------- 147
Cdd:cd05258   78 IHTAAQPSVTTSAssPRLDF-ETNALGTLNVLEAARQHAPNApFIFTSTNKVYGdlPNY-----LPLEELETRyelapeg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 148 -------ESTWSDPY--PY--SKKMAEKAVL---AANGsmlknggtLQTCALRPMCIYGERsQF-------LSNTIIKAL 206
Cdd:cd05258  152 wspagisESFPLDFShsLYgaSKGAADQYVQeygRIFG--------LKTVVFRCGCLTGPR-QFgtedqgwVAYFLKCAV 222

                 ...
gi 240120136 207 KNK 209
Cdd:cd05258  223 TGK 225
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
7-130 1.86e-09

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 58.08  E-value: 1.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKVFKpeTREQFFNLGTSIK-VTVLEGDILDTQYLRrACQGISVVIHTAAI 85
Cdd:cd05234    3 LVTGGAGFIGSHLVDRLLEEGN--EVVVVDNLSS--GRRENIEPEFENKaFRFVKRDLLDTADKV-AKKDGDTVFHLAAN 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 240120136  86 IDVT-GVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAG 130
Cdd:cd05234   78 PDVRlGATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSSTVYG 123
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
8-268 3.38e-09

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 57.72  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAIID 87
Cdd:PLN02986  10 VTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQAIEGCDAVFHTASPVF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  88 VTGVIPRQTILDVNLKGTQNLLEACIQ-ASVPAFIFSSSVDVA-------GPNSYKDIVLNGHEDEHRES-TWsdpYPYS 158
Cdd:PLN02986  90 FTVKDPQTELIDPALKGTINVLNTCKEtPSVKRVILTSSTAAVlfrqppiEANDVVDETFFSDPSLCRETkNW---YPLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 159 KKMAEKAVLaangSMLKNGGtLQTCALRPMCIYGERSQFLSNTIIKALKNkFIlrgGGKFSTANPVY----VGNVAWAHI 234
Cdd:PLN02986 167 KILAENAAW----EFAKDNG-IDMVVLNPGFICGPLLQPTLNFSVELIVD-FI---NGKNLFNNRFYrfvdVRDVALAHI 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 240120136 235 LAArglrnpkKSPNIQGEFYYisdDTPHQSYDDL 268
Cdd:PLN02986 238 KAL-------ETPSANGRYII---DGPIMSVNDI 261
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
7-167 3.46e-09

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. 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: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 57.24  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQE--KDLEEIRVLDKVFKPETREQFFNLGTSIKVTVleGDILDTQYLRRACQGISVVIHTAA 84
Cdd:cd05193    2 LVTGASGFVASHVVEQLLERgyKVRATVRDPSKVKKVNHLLDLDAKPGRLELAV--ADLTDEQSFDEVIKGCAGVFHVAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGVIPRQTILDvNLKGTQNLLEACIQA-SVPAFIFSSSVDVAGPNSykdivLNGHEDEHRESTWSDP--------- 154
Cdd:cd05193   80 PVSFSSKDPNEVIKP-AIGGTLNALKAAAAAkSVKRFVLTSSAGSVLIPK-----PNVEGIVLDEKSWNLEefdsdpkks 153
                        170
                 ....*....|....*.
gi 240120136 155 ---YPYSKKMAEKAVL 167
Cdd:cd05193  154 awvYAASKTLAEKAAW 169
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
7-125 1.59e-08

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. 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: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 55.40  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDKVFKPETreqfFNLGtsiKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:cd05264    3 LIVGGNGFIGSHLVDALLEEG--PQVRVFDRSIPPYE----LPLG---GVDYIKGDYENRADLESALVGIDTVIHLASTT 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 240120136  87 dVTGVIPRQTILDV--NLKGTQNLLEACIQASVPAFIFSSS 125
Cdd:cd05264   74 -NPATSNKNPILDIqtNVAPTVQLLEACAAAGIGKIIFASS 113
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-166 2.55e-08

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 53.38  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   10 GAGGFLGQRIIQLLVQEKDleEIRVLdkVFKPETREQFFNLGtsiKVTVLEGDILDTQYLRRACQGISVVIHTAAIIDVT 89
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGH--EVTAL--VRNPEKLADLEDHP---GVEVVDGDVLDPDDLAEALAGQDAVISALGGGGTD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   90 gviprqtildvnLKGTQNLLEACIQASVPAFIFSSSVDVagpnsykdivlnGHEDEHRESTWSD----PYPYSKKMAEKA 165
Cdd:pfam13460  74 ------------ETGAKNIIDAAKAAGVKRFVLVSSLGV------------GDEVPGPFGPWNKemlgPYLAAKRAAEEL 129

                  .
gi 240120136  166 V 166
Cdd:pfam13460 130 L 130
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
7-194 3.85e-08

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. 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: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 54.41  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDkVFKPETREQffnlgTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:cd05273    4 LVTGAGGFIGSHLAERLKAEG--HYVRGAD-WKSPEHMTQ-----PTDDDEFHLVDLREMENCLKATEGVDHVFHLAADM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  87 DVTGVIPRQ--TILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAgPNSYKDIVLNG--HEDEHRESTWSDPYPYSKKMA 162
Cdd:cd05273   76 GGMGYIQSNhaVIMYNNTLINFNMLEAARINGVERFLFASSACVY-PEFKQLETTVVrlREEDAWPAEPQDAYGWEKLAT 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 240120136 163 EKAVLAANGSMlknggTLQTCALRPMCIYGER 194
Cdd:cd05273  155 ERLCQHYNEDY-----GIETRIVRFHNIYGPR 181
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
7-238 3.87e-08

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 53.98  E-value: 3.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLvQEKDLEeirVldkvfkpetreqffnLGTSIKvtvlEGDILDTQYLRRACQGIS--VVIHTAA 84
Cdd:COG1091    3 LVTGANGQLGRALVRLL-AERGYE---V---------------VALDRS----ELDITDPEAVAALLEEVRpdVVINAAA 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGV-IPRQTILDVNLKGTQNLLEACIQASVPaFIFSSSvdvagpnsykDIVLNGHEDE-HREstwSDP------YP 156
Cdd:COG1091   60 YTAVDKAeSEPELAYAVNATGPANLAEACAELGAR-LIHIST----------DYVFDGTKGTpYTE---DDPpnplnvYG 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 157 YSKKMAEKAVLAANGsmlknggtlQTCALRPMCIYGERSQ-FLsNTIIKALKNKFILRG-----GgkfstaNPVYVGNVA 230
Cdd:COG1091  126 RSKLAGEQAVRAAGP---------RHLILRTSWVYGPHGKnFV-KTMLRLLKEGEELRVvddqiG------SPTYAADLA 189
                        250
                 ....*....|
gi 240120136 231 WA--HILAAR 238
Cdd:COG1091  190 RAilALLEKD 199
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
7-125 1.12e-07

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 52.94  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKV---FKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGIS--VVIH 81
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGY--EVHGIVRRsssFNTGRLEHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVQpdEIYN 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 240120136   82 TAAIIDVTGVI--PRQTIlDVNLKGTQNLLEACIQASVPA---FIFSSS 125
Cdd:pfam16363  79 LAAQSHVDVSFeqPEYTA-DTNVLGTLRLLEAIRSLGLEKkvrFYQAST 126
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
7-170 1.26e-07

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. 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: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 52.63  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLvQEKDLEEIRVldkvfkPETREQFFNLgtsikvtvlegDILDTQYLRRACQGIS--VVIHTAA 84
Cdd:cd05254    3 LITGATGMLGRALVRLL-KERGYEVIGT------GRSRASLFKL-----------DLTDPDAVEEAIRDYKpdVIINCAA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  85 IIDVTGV--IPRQTILdVNLKGTQNLLEACIQASVPAFIFSSsvdvagpnsykDIVLNGHEDEHRESTWSDP---YPYSK 159
Cdd:cd05254   65 YTRVDKCesDPELAYR-VNVLAPENLARAAKEVGARLIHIST-----------DYVFDGKKGPYKEEDAPNPlnvYGKSK 132
                        170
                 ....*....|.
gi 240120136 160 KMAEKAVLAAN 170
Cdd:cd05254  133 LLGEVAVLNAN 143
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
7-122 3.41e-07

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 50.24  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLdkVFKPEtREQFFNLGtsikVTVLEGDILDTQYLRRACQGISVVIHTAAii 86
Cdd:COG2910    3 AVIGATGRVGSLIVREALARGH--EVTAL--VRNPE-KLPDEHPG----LTVVVGDVLDPAAVAEALAGADAVVSALG-- 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 240120136  87 dvtgvIPRQTILDVNLKGTQNLLEACIQASVPAFIF 122
Cdd:COG2910   72 -----AGGGNPTTVLSDGARALIDAMKAAGVKRLIV 102
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
8-236 4.47e-07

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 51.18  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVqekdLEEIRVLDKVFKPETREQFFNL----GTSIKVTVLEGDILDTQYLRRACQGISVVIHTA 83
Cdd:PLN02989  10 VTGASGYIASWIVKLLL----FRGYTINATVRDPKDRKKTDHLlaldGAKERLKLFKADLLDEGSFELAIDGCETVFHTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AIIDVT-GVIPRQTILDVNLKGTQNLLEACIQ-ASVPAFIFSSSVDVA-------GPNSYKDivlnghedehrESTWSDP 154
Cdd:PLN02989  86 SPVAITvKTDPQVELINPAVNGTINVLRTCTKvSSVKRVILTSSMAAVlapetklGPNDVVD-----------ETFFTNP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 155 ---------YPYSKKMAEKAVLaangsMLKNGGTLQTCALRPMCIYGERSQFLSNTIIKALKNkfILRGGGKFSTANPVY 225
Cdd:PLN02989 155 sfaeerkqwYVLSKTLAEDAAW-----RFAKDNEIDLIVLNPGLVTGPILQPTLNFSVAVIVE--LMKGKNPFNTTHHRF 227
                        250
                 ....*....|...
gi 240120136 226 VG--NVAWAHILA 236
Cdd:PLN02989 228 VDvrDVALAHVKA 240
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
7-161 4.49e-07

ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. 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: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 51.15  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLvQEKDLEEIRVLDKvFKPETReqFFNL-GTSIkvtvleGDILDTQYLRRACQG------ISVV 79
Cdd:cd05248    3 IVTGGAGFIGSNLVKAL-NERGITDILVVDN-LSNGEK--FKNLvGLKI------ADYIDKDDFKDWVRKgdenfkIEAI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  80 IHTAAIIDVT---GVIprqtILDVNLKGTQNLLEACIQASVPaFIFSSSVDVagpnsYKDIVLNGHEDEHRESTWS-DPY 155
Cdd:cd05248   73 FHQGACSDTTetdGKY----MMDNNYQYTKELLHYCLEKKIR-FIYASSAAV-----YGNGSLGFAEDIETPNLRPlNVY 142

                 ....*.
gi 240120136 156 PYSKKM 161
Cdd:cd05248  143 GYSKLL 148
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
7-175 5.14e-07

CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4,6-dehydratase, an extended SDR, which catalyzes the conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended 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: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 50.78  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLvqeKDLEEIrVLDKVFKPETREQFFNLGT--SIKVTVlEGDILDTQYLRRACQGI--SVVIHT 82
Cdd:cd05252    8 LVTGHTGFKGSWLSLWL---QELGAK-VIGYSLDPPTNPNLFELANldNKISST-RGDIRDLNALREAIREYepEIVFHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  83 AA--IIDVTGVIPRQTIlDVNLKGTQNLLEACIQA-SVPAFIFSSSVDVagpnsYKDivlnghedehRESTW-------- 151
Cdd:cd05252   83 AAqpLVRLSYKDPVETF-ETNVMGTVNLLEAIRETgSVKAVVNVTSDKC-----YEN----------KEWGWgyrendpl 146
                        170       180
                 ....*....|....*....|....*.
gi 240120136 152 --SDPYPYSKKMAEKAVLAANGSMLK 175
Cdd:cd05252  147 ggHDPYSSSKGCAELIISSYRNSFFN 172
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
7-164 1.51e-06

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 49.43  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRI-IQLLVQEKDleeIRVLDkvfkpetreqffNLGTSiKVTVL--------------EGDILDTQYLRR 71
Cdd:PRK10675   4 LVTGGSGYIGSHTcVQLLQNGHD---VVILD------------NLCNS-KRSVLpvierlggkhptfvEGDIRNEALLTE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  72 --ACQGISVVIHTAAIIDVtGVIPRQTI--LDVNLKGTQNLLEACIQASVPAFIFSSSVDVagpnsYKDIVLNGHEDEHR 147
Cdd:PRK10675  68 ilHDHAIDTVIHFAGLKAV-GESVQKPLeyYDNNVNGTLRLISAMRAANVKNLIFSSSATV-----YGDQPKIPYVESFP 141
                        170
                 ....*....|....*..
gi 240120136 148 ESTWSDPYPYSKKMAEK 164
Cdd:PRK10675 142 TGTPQSPYGKSKLMVEQ 158
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
7-136 1.53e-06

L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended 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: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 49.23  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVfKPETREqfFNLGTSIKVtvlegDILDTQYLRRACQ--GISVVIHTAA 84
Cdd:cd05272    3 LITGGLGQIGSELAKLLRKRYGKDNVIASDIR-KPPAHV--VLSGPFEYL-----DVLDFKSLEEIVVnhKITWIIHLAA 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240120136  85 IIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIfSSSVDVAGPNSYKD 136
Cdd:cd05272   75 LLSAVGEKNPPLAWDVNMNGLHNVLELAREHNLRIFV-PSTIGAFGPTTPRN 125
PLN02686 PLN02686
cinnamoyl-CoA reductase
8-242 2.52e-06

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 49.01  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQ-----------EKDLEEIRVLdkvfkpetrEQFFNLGTSIK-VTVLEGDILDTQYLRRACQG 75
Cdd:PLN02686  58 VTGGVSFLGLAIVDRLLRhgysvriavdtQEDKEKLREM---------EMFGEMGRSNDgIWTVMANLTEPESLHEAFDG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  76 ISVVIHTAAIID---VTGVIPRQTILDVnlKGTQNLLEACIQ-ASVPAFIFSSS----VDVAGPNSYKDIVLNghedehr 147
Cdd:PLN02686 129 CAGVFHTSAFVDpagLSGYTKSMAELEA--KASENVIEACVRtESVRKCVFTSSllacVWRQNYPHDLPPVID------- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 148 ESTWSDP---------YPYSKKMAEKAVL-AANGSMLKnggtLQT-CalrPMCIYG----ERSqflSNTIIKALKNKFIL 212
Cdd:PLN02686 200 EESWSDEsfcrdnklwYALGKLKAEKAAWrAARGKGLK----LATiC---PALVTGpgffRRN---STATIAYLKGAQEM 269
                        250       260       270
                 ....*....|....*....|....*....|
gi 240120136 213 RGGGKFSTANpvyVGNVAWAHILAARGLRN 242
Cdd:PLN02686 270 LADGLLATAD---VERLAEAHVCVYEAMGN 296
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
7-259 3.69e-06

Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 48.17  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIiqllvqekdLEEIRVLDKV------FKPETREQFFNLGTSI------KVTVLEGDILDTQYLRRACQ 74
Cdd:PRK15181  19 LITGVAGFIGSGL---------LEELLFLNQTvigldnFSTGYQHNLDDVRTSVseeqwsRFIFIQGDIRKFTDCQKACK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  75 GISVVIHTAAIidvtGVIPRQ-----TILDVNLKGTQNLLEACIQASVPAFIFSSSvdvagPNSYKDivlngHED----E 145
Cdd:PRK15181  90 NVDYVLHQAAL----GSVPRSlkdpiATNSANIDGFLNMLTAARDAHVSSFTYAAS-----SSTYGD-----HPDlpkiE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 146 HRESTWSDPYPYSKKMAEkavLAANgsMLKNGGTLQTCALRPMCIYGER-------SQFLSNTIIKALKNKFILRGGGKF 218
Cdd:PRK15181 156 ERIGRPLSPYAVTKYVNE---LYAD--VFARSYEFNAIGLRYFNVFGRRqnpngaySAVIPRWILSLLKDEPIYINGDGS 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 240120136 219 STANPVYVGNVAWAHILAA--RGLRNPKKSPNIQ-------GEFYYISDD 259
Cdd:PRK15181 231 TSRDFCYIENVIQANLLSAttNDLASKNKVYNVAvgdrtslNELYYLIRD 280
PLN02260 PLN02260
probable rhamnose biosynthetic enzyme
7-168 4.64e-06

probable rhamnose biosynthetic enzyme


Pssm-ID: 215146 [Multi-domain]  Cd Length: 668  Bit Score: 48.59  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDT---QYLRRAcQGISVVIHTA 83
Cdd:PLN02260  10 LITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASAdlvNYLLIT-EGIDTIMHFA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  84 AiidvtgviprQTILD-----------VNLKGTQNLLEAC-IQASVPAFIFSSSVDVAGPNSYKDIVLNgHEDEHRESTw 151
Cdd:PLN02260  89 A----------QTHVDnsfgnsfeftkNNIYGTHVLLEACkVTGQIRRFIHVSTDEVYGETDEDADVGN-HEASQLLPT- 156
                        170
                 ....*....|....*..
gi 240120136 152 sDPYPYSKKMAEKAVLA 168
Cdd:PLN02260 157 -NPYSATKAGAEMLVMA 172
PRK07201 PRK07201
SDR family oxidoreductase;
7-166 6.07e-06

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 48.02  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLdkvFKPETREQFFNL----GTSiKVTVLEGDI------LDTQYLRRACQgI 76
Cdd:PRK07201   4 FVTGGTGFIGRRLVSRLLDRRREATVHVL---VRRQSLSRLEALaaywGAD-RVVPLVGDLtepglgLSEADIAELGD-I 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  77 SVVIHTAAIIDVTGVIPRQTIldVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPnsykdivlngHEDEHRESTWS---- 152
Cdd:PRK07201  79 DHVVHLAAIYDLTADEEAQRA--ANVDGTRNVVELAERLQAATFHHVSSIAVAGD----------YEGVFREDDFDegqg 146
                        170
                 ....*....|....*.
gi 240120136 153 --DPYPYSKKMAEKAV 166
Cdd:PRK07201 147 lpTPYHRTKFEAEKLV 162
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
8-236 6.49e-06

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 47.40  E-value: 6.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQE--------------KDLEEIRVLDKVfkpETREQFFnlgtsiKVTVLEGDILDTqylrrAC 73
Cdd:PLN02662   9 VTGASGYIASWLVKLLLQRgytvkatvrdpndpKKTEHLLALDGA---KERLHLF------KANLLEEGSFDS-----VV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  74 QGISVVIHTAA--IIDVTGviPRQTILDVNLKGTQNLLEACIQA-SVPAFIFSSS---VDVAGPNSYKDIVLngheDEhr 147
Cdd:PLN02662  75 DGCEGVFHTASpfYHDVTD--PQAELIDPAVKGTLNVLRSCAKVpSVKRVVVTSSmaaVAYNGKPLTPDVVV----DE-- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 148 esTW-SDP---------YPYSKKMAEKAvlAANGSMlKNGgtLQTCALRPMCIYGERSQFLSNTIIKALKNkfILRGGGK 217
Cdd:PLN02662 147 --TWfSDPafceesklwYVLSKTLAEEA--AWKFAK-ENG--IDMVTINPAMVIGPLLQPTLNTSAEAILN--LINGAQT 217
                        250       260
                 ....*....|....*....|.
gi 240120136 218 F--STANPVYVGNVAWAHILA 236
Cdd:PLN02662 218 FpnASYRWVDVRDVANAHIQA 238
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
7-133 1.31e-05

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 46.14  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDLeEIRVLdkvFKPETRE--QFFNLGtsikVTVLEGDILDTQYLRRACQGISVVIHTAA 84
Cdd:cd05259    3 AIAGATGTLGGPIVSALLASPGF-TVTVL---TRPSSTSsnEFQPSG----VKVVPVDYASHESLVAALKGVDAVISALG 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 240120136  85 IIDVtgviprqtildvnlkGTQ-NLLEACIQASVPAFI---FSSSVDVAGPNS 133
Cdd:cd05259   75 GAAI---------------GDQlKLIDAAIAAGVKRFIpseFGVDYDRIGALP 112
PLN02650 PLN02650
dihydroflavonol-4-reductase
8-168 2.23e-05

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 45.97  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVFKPETREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAIID 87
Cdd:PLN02650  10 VTGASGFIGSWLVMRLLERGYTVRATVRDPANVKKVKHLLDLPGATTRLTLWKADLAVEGSFDDAIRGCTGVFHVATPMD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  88 VTGVIPRQTILDVNLKGTQNLLEACIQA-SVPAFIFSSS---VDVagpnsykdivlngheDEHR-----ESTWSD----- 153
Cdd:PLN02650  90 FESKDPENEVIKPTVNGMLSIMKACAKAkTVRRIVFTSSagtVNV---------------EEHQkpvydEDCWSDldfcr 154
                        170       180
                 ....*....|....*....|..
gi 240120136 154 -------PYPYSKKMAEKAVLA 168
Cdd:PLN02650 155 rkkmtgwMYFVSKTLAEKAAWK 176
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
7-133 2.26e-05

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 45.34  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVqeKDLEEIRVLdkVFKPETREQFFNLGtsikVTVLEGDILDTQYLRRACQGISVVIhtaaII 86
Cdd:cd05269    2 LVTGATGKLGTAVVELLL--AKVASVVAL--VRNPEKAKAFAADG----VEVRQGDYDDPETLERAFEGVDRLL----LI 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 240120136  87 DVTGVIPRqtildvnLKGTQNLLEACIQASVpAFIFSSSVDVAGPNS 133
Cdd:cd05269   70 SPSDLEDR-------IQQHKNFIDAAKQAGV-KHIVYLSASGADEDS 108
PLN00198 PLN00198
anthocyanidin reductase; Provisional
8-165 6.24e-05

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 44.49  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKdleeIRVLDKVFKPETRE------QFFNLGtsiKVTVLEGDILDTQYLRRACQGISVVIH 81
Cdd:PLN00198  14 VIGGTGFLASLLIKLLLQKG----YAVNTTVRDPENQKkiahlrALQELG---DLKIFGADLTDEESFEAPIAGCDLVFH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  82 TAAIIDVTGVIPRQTILDVNLKGTQNLLEACIQA-SVPAFIFSSSVDVAGPNSykdivLNGHEDEHRESTWSD------- 153
Cdd:PLN00198  87 VATPVNFASEDPENDMIKPAIQGVHNVLKACAKAkSVKRVILTSSAAAVSINK-----LSGTGLVMNEKNWTDvefltse 161
                        170
                 ....*....|....*..
gi 240120136 154 -----PYPYSKKMAEKA 165
Cdd:PLN00198 162 kpptwGYPASKTLAEKA 178
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
6-81 6.80e-05

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 44.26  E-value: 6.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240120136   6 CLVTGAGGFLGQRIIQLLVQEKDleEIRVLDKvfkpeTREQFFNLGTSIKVTVLEGDILDTQYLRRACQGISVVIH 81
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGH--QVRALVR-----SPEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYY 69
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
8-126 8.15e-05

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 44.04  E-value: 8.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKdleeIRVLDKVFKPETREQFFNLGTSI-KVTVLEGDILDTQYLRRACQGISVVIHTAAI- 85
Cdd:PLN02896  15 VTGATGYIGSWLVKLLLQRG----YTVHATLRDPAKSLHLLSKWKEGdRLRLFRADLQEEGSFDEAVKGCDGVFHVAASm 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 240120136  86 -IDVTGV------IPRQTILDVNLKGTQNLLEACIQA-SVPAFIFSSSV 126
Cdd:PLN02896  91 eFDVSSDhnnieeYVQSKVIDPAIKGTLNVLKSCLKSkTVKRVVFTSSI 139
PRK05865 PRK05865
sugar epimerase family protein;
8-130 8.52e-05

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 44.65  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRII-QLLVQEKDLEEIrvldKVFKPETreqffnlgTSIKVTVLEGDILDTQYLRRACQGISVVIHTAAii 86
Cdd:PRK05865   5 VTGASGVLGRGLTaRLLSQGHEVVGI----ARHRPDS--------WPSSADFIAADIRDATAVESAMTGADVVAHCAW-- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 240120136  87 dvtgviPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAG 130
Cdd:PRK05865  71 ------VRGRNDHINIDGTANVLKAMAETGTGRIVFTSSGHQPR 108
PLN02214 PLN02214
cinnamoyl-CoA reductase
3-235 1.97e-04

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 42.82  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   3 GWSCLVTGAGGFLGQRIIQLLVQEKDLEE--IRVLDKVFKPETREQffnLGTSIKVTVLEGDILDTQYLRRACQGISVVI 80
Cdd:PLN02214  10 GKTVCVTGAGGYIASWIVKILLERGYTVKgtVRNPDDPKNTHLREL---EGGKERLILCKADLQDYEALKAAIDGCDGVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  81 HTAAIIDVTgviPRQtILDVNLKGTQNLLEACIQASVPAFIFSSSVDVA--GPNSYKDIVLNghedehrESTWSDP---- 154
Cdd:PLN02214  87 HTASPVTDD---PEQ-MVEPAVNGAKFVINAAAEAKVKRVVITSSIGAVymDPNRDPEAVVD-------ESCWSDLdfck 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 155 -----YPYSKKMAEKAVLaangSMLKNGGtLQTCALRPMCIYGERsqfLSNTIIKALKN--KFILRGGGKFSTANPVYVG 227
Cdd:PLN02214 156 ntknwYCYGKMVAEQAAW----ETAKEKG-VDLVVLNPVLVLGPP---LQPTINASLYHvlKYLTGSAKTYANLTQAYVD 227
                        250
                 ....*....|
gi 240120136 228 --NVAWAHIL 235
Cdd:PLN02214 228 vrDVALAHVL 237
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
7-136 3.03e-04

ketoreductase (KR), subgroup 2, 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. 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. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. 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: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 42.74  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleeIRVL---------DKVFKPETREQFFNLGTSikVTVLEGDILDTQYLRRA----- 72
Cdd:cd08953  209 LVTGGAGGIGRALARALARRYG---ARLVllgrsplppEEEWKAQTLAALEALGAR--VLYISADVTDAAAVRRLlekvr 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  73 --CQGISVVIHTAAIIDvTGVIPRQT------ILDVNLKGTQNLLEACIQASVPAFIFSSSV----------DVAGPNSY 134
Cdd:cd08953  284 erYGAIDGVIHAAGVLR-DALLAQKTaedfeaVLAPKVDGLLNLAQALADEPLDFFVLFSSVsaffggagqaDYAAANAF 362

                 ..
gi 240120136 135 KD 136
Cdd:cd08953  363 LD 364
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
8-238 1.01e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 40.41  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   8 VTGAGGFLGQRIIQLLVQEKDleeiRVLDKVFKPETREQFFNLGTSikvtVLEGDILDTQYLRRACQGISVVIHTAAIID 87
Cdd:cd05262    5 VTGATGFIGSAVVRELVAAGH----EVVGLARSDAGAAKLEAAGAQ----VHRGDLEDLDILRKAAAEADAVIHLAFTHD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  88 VTgviPRQTILDVNLKGTQNLLEACIQASVPaFIFSSSVDVAGPnsykdivlNGHEDEHRESTWSDPYPYSKKMAEKAVL 167
Cdd:cd05262   77 FD---NFAQACEVDRRAIEALGEALRGTGKP-LIYTSGIWLLGP--------TGGQEEDEEAPDDPPTPAARAVSEAAAL 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240120136 168 AANGSMLKNGGTlqtcaLRPMCIYGERSQFLSNTIIKALKNKfilrggGKFStanpvYVGNV--AWA--HIL-AAR 238
Cdd:cd05262  145 ELAERGVRASVV-----RLPPVVHGRGDHGFVPMLIAIAREK------GVSA-----YVGDGknRWPavHRDdAAR 204
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7-246 1.04e-03

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: 41.20  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136     7 LVTGAGGFLGQRIIQLLVQEKDLEEIRVLDKVfKPETREQFFN--------LGT-----SIKVTVLEGD-------ILDT 66
Cdd:TIGR03443  975 FLTGATGFLGSFILRDLLTRRSNSNFKVFAHV-RAKSEEAGLErlrktgttYGIwdeewASRIEVVLGDlskekfgLSDE 1053
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    67 QYLRRACQgISVVIHTAAIidVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSY----KDIVLNGH 142
Cdd:TIGR03443 1054 KWSDLTNE-VDVIIHNGAL--VHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYvnlsDELVQAGG 1130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   143 ----EDEHRESTWSD---PYPYSKKMAEKAVLAANgsmlKNGgtLQTCALRPMCIYGERSQFLSNT---IIKALKNKFIL 212
Cdd:TIGR03443 1131 agipESDDLMGSSKGlgtGYGQSKWVAEYIIREAG----KRG--LRGCIVRPGYVTGDSKTGATNTddfLLRMLKGCIQL 1204
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 240120136   213 rggGK----FSTANPVYVGNVawAHILAARGLRNPKKS 246
Cdd:TIGR03443 1205 ---GLipniNNTVNMVPVDHV--ARVVVAAALNPPKES 1237
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
7-132 1.04e-03

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. 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: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 40.66  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVqEKDLEeirVLDKVFKPETREQ---FFNLGTSIKVTVLEGDILDTQYLRRACQGIS--VVIH 81
Cdd:cd05260    3 LITGITGQDGSYLAEFLL-EKGYE---VHGIVRRSSSFNTdriDHLYINKDRITLHYGDLTDSSSLRRAIEKVRpdEIYH 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240120136  82 TAAI--IDVTGVIPRQTiLDVNLKGTQNLLEACIQASVPA-FIFSSSVDVAGPN 132
Cdd:cd05260   79 LAAQshVKVSFDDPEYT-AEVNAVGTLNLLEAIRILGLDArFYQASSSEEYGKV 131
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-126 1.05e-03

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 39.77  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136     7 LVTGAGGFLGQRIIQLLVQE--KDLeeirVL------DKVFKPETREQFFNLGTSikVTVLEGDILDTQYLRRACQGISV 78
Cdd:smart00822   4 LITGGLGGLGRALARWLAERgaRRL----VLlsrsgpDAPGAAALLAELEAAGAR--VTVVACDVADRDALAAVLAAIPA 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240120136    79 -------VIHTAAIIDvTGVIPRQTILDVN------LKGTQNLLEACIQASVPAFIFSSSV 126
Cdd:smart00822  78 vegpltgVIHAAGVLD-DGVLASLTPERFAavlapkAAGAWNLHELTADLPLDFFVLFSSI 137
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
7-126 1.12e-03

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 39.47  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVqEKDLEEIRVL--DKVFKPETREQFFNL-GTSIKVTVLEGDILDTQYLRRACQGISV----- 78
Cdd:pfam08659   4 LITGGLGGLGRELARWLA-ERGARHLVLLsrSAAPRPDAQALIAELeARGVEVVVVACDVSDPDAVAALLAEIKAegppi 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240120136   79 --VIHTAAIIDvTGVIPRQTILDVN------LKGTQNLLEACIQASVPAFIFSSSV 126
Cdd:pfam08659  83 rgVIHAAGVLR-DALLENMTDEDWRrvlapkVTGTWNLHEATPDEPLDFFVLFSSI 137
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
7-122 2.20e-03

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. 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: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 39.41  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleEIRVLDKvFKPETREqffNLGTSIKVTVLEGDILDTQYLRRACQGIS--VVIHTAA 84
Cdd:cd08957    4 LITGGAGQIGSHLIEHLLERGH--QVVVIDN-FATGRRE---HLPDHPNLTVVEGSIADKALVDKLFGDFKpdAVVHTAA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 240120136  85 IIDvtgvIPRQTILD--VNLKGTQNLLEACIQASVPAFIF 122
Cdd:cd08957   78 AYK----DPDDWYEDtlTNVVGGANVVQAAKKAGVKRLIY 113
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
7-124 2.69e-03

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 38.86  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136    7 LVTGAGGFLGQRIIQLLVQEKdlEEIRVLDKVFKPETREQFFNLGtsikVTVLEGDILDTQYLRRACQGISVVihtaaiI 86
Cdd:pfam05368   2 LVFGATGQQGGSVVRASLKAG--HKVRALVRDPKSELAKSLKEAG----VELVKGDLDDKESLVEALKGVDVV------F 69
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 240120136   87 DVTGVIPRQTILDvnlkGTqNLLEACIQASVPAFIFSS 124
Cdd:pfam05368  70 SVTGFWAGKEIED----GK-KLADAAKEAGVKHFIPSS 102
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
7-131 3.05e-03

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 38.49  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEKDleeIRVLDKVFKPETREQFFNlgtsIKVTVLEGDILDTQYLRRACQGISVVIHTAAII 86
Cdd:cd05267    4 LILGANGEIAREATTMLLENSN---VELTLFLRNAHRLLHLKS----ARVTVVEGDALNSDDLKAAMRGQDVVYANLGGT 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 240120136  87 DVTgviprqtildvnlKGTQNLLEACIQASVPAFIFSSSV----DVAGP 131
Cdd:cd05267   77 DLD-------------QQAENVVQAMKAVGVKRLIWTTSLgiydEVPGK 112
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
5-274 4.19e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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 ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   5 SCLVTGAGGFLGQRIIQLLVQEKDleEIRVLD----KVFKPEtreqffnlgtsiKVTVLEGDILDTQYLRRACQGISVvi 80
Cdd:cd05265    2 KILIIGGTRFIGKALVEELLAAGH--DVTVFNrgrtKPDLPE------------GVEHIVGDRNDRDALEELLGGEDF-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136  81 htAAIIDVTGVIPRQtildvnlkgTQNLLEACiQASVPAFIFSSSVDV--AGPNSYKDIVLNGHEDEHRESTWSDpYPYS 158
Cdd:cd05265   66 --DVVVDTIAYTPRQ---------VERALDAF-KGRVKQYIFISSASVylKPGRVITESTPLREPDAVGLSDPWD-YGRG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136 159 KKMAEKAVLAANGsmlknggtLQTCALRPMCIYGERSQF--LSNTIIKALKNKFILRGGGKFSTANPVYVGNVAWAhILA 236
Cdd:cd05265  133 KRAAEDVLIEAAA--------FPYTIVRPPYIYGPGDYTgrLAYFFDRLARGRPILVPGDGHSLVQFIHVKDLARA-LLG 203
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 240120136 237 ARGlrNPKKSpniqGEFYYISDDTPHqSYDDLNYTLSK 274
Cdd:cd05265  204 AAG--NPKAI----GGIFNITGDEAV-TWDELLEACAK 234
PRK12826 PRK12826
SDR family oxidoreductase;
7-131 4.82e-03

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 38.36  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQEK------DLEEIRVldkvfkPETREQFFNLGTSIKVtvLEGDILDTQYLRRACQ------ 74
Cdd:PRK12826  10 LVTGAARGIGRAIAVRLAADGaevivvDICGDDA------AATAELVEAAGGKARA--RQVDVRDRAALKAAVAagvedf 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240120136  75 -GISVVIHTAAI--------IDVTGViprQTILDVNLKGTQNlleaCIQASVPAFIFS--------SSvdVAGP 131
Cdd:PRK12826  82 gRLDILVANAGIfpltpfaeMDDEQW---ERVIDVNLTGTFL----LTQAALPALIRAgggrivltSS--VAGP 146
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-113 7.88e-03

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 37.45  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120136   7 LVTGAGGFLGQRIIQLLVQE--------KDLEEIRvldkvfkpETREQFFNLGtsIKVTVLEGDILDTQYLRRACQ---- 74
Cdd:PRK05653   9 LVTGASRGIGRAIALRLAADgakvviydSNEEAAE--------ALAAELRAAG--GEARVLVFDVSDEAAVRALIEaave 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 240120136  75 ---GISVVIHTAAIIDVtGVIPR------QTILDVNLKGTQNLLEACI 113
Cdd:PRK05653  79 afgALDILVNNAGITRD-ALLPRmseedwDRVIDVNLTGTFNVVRAAL 125
 
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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