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Conserved domains on  [gi|145339118|ref|NP_190041|]
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fatty acid reductase 5 [Arabidopsis thaliana]

Protein Classification

PLN02996 family protein( domain architecture ID 11477349)

PLN02996 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02996 PLN02996
fatty acyl-CoA reductase
1-495 0e+00

fatty acyl-CoA reductase


:

Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 947.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   1 MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGdEKLN 80
Cdd:PLN02996   1 EEGSCVQFLENKTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHDEVIGKDLFKVLREKLG-ENLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  81 TLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHV 160
Cdd:PLN02996  80 SLISEKVTPVPGDISYDDLGVKDSNLREEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKMLLHV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 161 STAYVCGEKPGLIPEKPFIMEEIRNENGlQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVF 240
Cdd:PLN02996 160 STAYVCGEKSGLILEKPFHMGETLNGNR-KLDINEEKKLVKEKLKELNEQDASEEEITQAMKDLGMERAKLHGWPNTYVF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 241 TKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMI 320
Cdd:PLN02996 239 TKAMGEMLLGNFKENLPLVIIRPTMITSTYKEPFPGWIEGLRTIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 321 TAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQL 400
Cdd:PLN02996 319 VAMAAHAGGQGSEIIYHVGSSLKNPVKFSNLHDFAYRYFSKNPWINKEGSPVKVGKGTILSTMASFSLYMTIRYLLPLKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 401 LKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEikNTEKLMFDFDPKGINWGDY 480
Cdd:PLN02996 399 LQLVNIILPKRYGDKYTDLNRKIKLVMRLVDLYKPYVFFKGIFDDTNTEKLRIKRKETG--KEEADMFDFDPKSIDWEDY 476
                        490
                 ....*....|....*
gi 145339118 481 LTNIHISGLVTHVLK 495
Cdd:PLN02996 477 MTNVHIPGLVKYVLK 491
 
Name Accession Description Interval E-value
PLN02996 PLN02996
fatty acyl-CoA reductase
1-495 0e+00

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 947.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   1 MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGdEKLN 80
Cdd:PLN02996   1 EEGSCVQFLENKTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHDEVIGKDLFKVLREKLG-ENLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  81 TLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHV 160
Cdd:PLN02996  80 SLISEKVTPVPGDISYDDLGVKDSNLREEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKMLLHV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 161 STAYVCGEKPGLIPEKPFIMEEIRNENGlQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVF 240
Cdd:PLN02996 160 STAYVCGEKSGLILEKPFHMGETLNGNR-KLDINEEKKLVKEKLKELNEQDASEEEITQAMKDLGMERAKLHGWPNTYVF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 241 TKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMI 320
Cdd:PLN02996 239 TKAMGEMLLGNFKENLPLVIIRPTMITSTYKEPFPGWIEGLRTIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 321 TAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQL 400
Cdd:PLN02996 319 VAMAAHAGGQGSEIIYHVGSSLKNPVKFSNLHDFAYRYFSKNPWINKEGSPVKVGKGTILSTMASFSLYMTIRYLLPLKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 401 LKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEikNTEKLMFDFDPKGINWGDY 480
Cdd:PLN02996 399 LQLVNIILPKRYGDKYTDLNRKIKLVMRLVDLYKPYVFFKGIFDDTNTEKLRIKRKETG--KEEADMFDFDPKSIDWEDY 476
                        490
                 ....*....|....*
gi 145339118 481 LTNIHISGLVTHVLK 495
Cdd:PLN02996 477 MTNVHIPGLVKYVLK 491
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
12-363 3.90e-130

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: 380.49  E-value: 3.90e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  12 KTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELfkvlrqnLGDEKLNTLLYEKVVSVP 91
Cdd:cd05236    1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLF-------DRGRNLNPLFESKIVPIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  92 GDIATDQLGINDSHLrERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPg 171
Cdd:cd05236   74 GDLSEPNLGLSDEDL-QTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQ- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 172 LIPEKPFIMEEIRNENglqldinlerelmkqrlkelneqdcseEDITLSMKELGMERA---KLHGWPNTYVFTKSMGEML 248
Cdd:cd05236  152 LIEEKVYPPPADPEKL---------------------------IDILELMDDLELERAtpkLLGGHPNTYTFTKALAERL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 249 LGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAG 328
Cdd:cd05236  205 VLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAAYSGV 284
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 145339118 329 G-SGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNP 363
Cdd:cd05236  285 RkPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP 320
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
16-319 1.68e-97

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: 294.52  E-value: 1.68e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   16 VTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQnlgdeklntLLYEKVVSVPGDIA 95
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLK---------EALERIVPVAGDLS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   96 TDQLGInDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPE 175
Cdd:pfam07993  72 EPNLGL-SEEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGGLVEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  176 KPFIMEEirnenglqldinlerelmkqrlkelneqdcseeditLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGK-HKE 254
Cdd:pfam07993 151 KPYPEGE------------------------------------DDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREaARR 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145339118  255 NLPLVIIRPTMITstlSEPFPGWIEGLR-TVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAM 319
Cdd:pfam07993 195 GLPVVIYRPSIIT---GEPKTGWINNFDfGPRGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
12-349 3.59e-38

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: 140.34  E-value: 3.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  12 KTILVTGATGFLAKVFVEKILRVQPNvkKLYLLVRASDNEAATKRLRtEVFEkelfkvlRQNLGDEKLNtllyEKVVSVP 91
Cdd:COG3320    1 RTVLLTGATGFLGAHLLRELLRRTDA--RVYCLVRASDEAAARERLE-ALLE-------RYGLWLELDA----SRVVVVA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  92 GDIATDQLGINDSHlRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCvKVQLLLHVSTAYVCG--EK 169
Cdd:COG3320   67 GDLTQPRLGLSEAE-FQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATG-RLKPFHYVSTIAVAGpaDR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 170 PGLIPEKPFIMEEirnenglqldinlerelmkqrlkelneqdcseeditlsmkelgmeraklhGWPNTYVFTKSMGEMLL 249
Cdd:COG3320  145 SGVFEEDDLDEGQ--------------------------------------------------GFANGYEQSKWVAEKLV 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 250 GK-HKENLPLVIIRPTMIT---STlsepfpGWIEGLRTVDSVIIAYGKgvLKCFLVDVNSVCDMIPVDMVANAmITAAAK 325
Cdd:COG3320  175 REaRERGLPVTIYRPGIVVgdsRT------GETNKDDGFYRLLKGLLR--LGAAPGLGDARLNLVPVDYVARA-IVHLSR 245
                        330       340
                 ....*....|....*....|....
gi 145339118 326 HAGGSGvhMVYHVgsSHQNPVTFG 349
Cdd:COG3320  246 QPEAAG--RTFHL--TNPQPLSLG 265
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
13-358 4.75e-18

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: 85.54  E-value: 4.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   13 TILVTGATGFLAKVFVEKILRVQPNvKKLYLLVRASDNEAATKRLRtevfekELFKVLRqnLGDEKlntLLYEKVVSVPG 92
Cdd:TIGR01746   1 TVLLTGATGFLGAYLLEELLRRSTR-AKVICLVRADSEEHAMERLR------EALRSYR--LWHEN---LAMERIEVVAG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   93 DIATDQLGINDSHLrERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKcVKVQLLLHVSTAYVC--GEKP 170
Cdd:TIGR01746  69 DLSKPRLGLSDAEW-ERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAAS-GRAKPLHYVSTISVGaaIDLS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  171 GLIPEkpfimeeirnenglqldinlerelmkqrlkelneqdcsEEDItlsmkelgmeRAKLHGWPNTYVFTKSMGEMLLG 250
Cdd:TIGR01746 147 TGVTE--------------------------------------DDAT----------VTPYPGLAGGYTQSKWVAELLVR 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  251 KHKEN-LPLVIIRPTMITstlSEPFPGWIEG----LRTVDSViIAYGKgVLKCflvDVNSVcDMIPVDMVANAmITAAAK 325
Cdd:TIGR01746 179 EASDRgLPVTIVRPGRIL---GDSYTGAWNSsdilWRMVKGC-LALGA-YPQS---PELTE-DLTPVDFVARA-IVALSS 248
                         330       340       350
                  ....*....|....*....|....*....|...
gi 145339118  326 HAGGSGVHMVYHVgsSHQNPVTFGEIHEIAVRY 358
Cdd:TIGR01746 249 RPAASAGGIVFHV--VNPNPVPLDEFLEWLERA 279
 
Name Accession Description Interval E-value
PLN02996 PLN02996
fatty acyl-CoA reductase
1-495 0e+00

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 947.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   1 MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGdEKLN 80
Cdd:PLN02996   1 EEGSCVQFLENKTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHDEVIGKDLFKVLREKLG-ENLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  81 TLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHV 160
Cdd:PLN02996  80 SLISEKVTPVPGDISYDDLGVKDSNLREEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKKCVKVKMLLHV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 161 STAYVCGEKPGLIPEKPFIMEEIRNENGlQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVF 240
Cdd:PLN02996 160 STAYVCGEKSGLILEKPFHMGETLNGNR-KLDINEEKKLVKEKLKELNEQDASEEEITQAMKDLGMERAKLHGWPNTYVF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 241 TKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMI 320
Cdd:PLN02996 239 TKAMGEMLLGNFKENLPLVIIRPTMITSTYKEPFPGWIEGLRTIDSVIVGYGKGKLTCFLADPNSVLDVIPADMVVNAMI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 321 TAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQL 400
Cdd:PLN02996 319 VAMAAHAGGQGSEIIYHVGSSLKNPVKFSNLHDFAYRYFSKNPWINKEGSPVKVGKGTILSTMASFSLYMTIRYLLPLKA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 401 LKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEikNTEKLMFDFDPKGINWGDY 480
Cdd:PLN02996 399 LQLVNIILPKRYGDKYTDLNRKIKLVMRLVDLYKPYVFFKGIFDDTNTEKLRIKRKETG--KEEADMFDFDPKSIDWEDY 476
                        490
                 ....*....|....*
gi 145339118 481 LTNIHISGLVTHVLK 495
Cdd:PLN02996 477 MTNVHIPGLVKYVLK 491
PLN02503 PLN02503
fatty acyl-CoA reductase 2
6-495 1.03e-151

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 445.85  E-value: 1.03e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   6 VQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGdEKLNTLLYE 85
Cdd:PLN02503 114 AEFLRGKNFLITGATGFLAKVLIEKILRTNPDVGKIYLLIKAKDKEAAIERLKNEVIDAELFKCLQETHG-KSYQSFMLS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  86 KVVSVPGDIATDQLGInDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYV 165
Cdd:PLN02503 193 KLVPVVGNVCESNLGL-EPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKLKLFLQVSTAYV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 166 CGEKPGLIPEKPFIM-EEIRNENGLQ---------LDINLEREL-MKQRLKELNEQDCSEEditlsMKELGMERAKLHGW 234
Cdd:PLN02503 272 NGQRQGRIMEKPFRMgDCIARELGISnslphnrpaLDIEAEIKLaLDSKRHGFQSNSFAQK-----MKDLGLERAKLYGW 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 235 PNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDM 314
Cdd:PLN02503 347 QDTYVFTKAMGEMVINSMRGDIPVVIIRPSVIESTWKDPFPGWMEGNRMMDPIVLYYGKGQLTGFLADPNGVLDVVPADM 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 315 VANAMITAAAKH--AGGSGVHmVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYM-- 390
Cdd:PLN02503 427 VVNATLAAMAKHggAAKPEIN-VYQIASSVVNPLVFQDLARLLYEHYKSSPYMDSKGRPIHVPPMKLFSSMEDFSSHLwr 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 391 --TLRYKL-------PLQLLKLVDIIypwrngdkygdkNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEeik 461
Cdd:PLN02503 506 daLLRSGLagmsssdRKLSQKLENIC------------AKSVEQAKYLASIYEPYTFYGGRFDNSNTQRLMERMSEE--- 570
                        490       500       510
                 ....*....|....*....|....*....|....
gi 145339118 462 ntEKLMFDFDPKGINWGDYLTNIHISGLVTHVLK 495
Cdd:PLN02503 571 --EKAEFGFDVGSIDWRDYITNVHIPGLRRHVMK 602
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
12-363 3.90e-130

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: 380.49  E-value: 3.90e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  12 KTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELfkvlrqnLGDEKLNTLLYEKVVSVP 91
Cdd:cd05236    1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLF-------DRGRNLNPLFESKIVPIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  92 GDIATDQLGINDSHLrERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPg 171
Cdd:cd05236   74 GDLSEPNLGLSDEDL-QTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYVNGDRQ- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 172 LIPEKPFIMEEIRNENglqldinlerelmkqrlkelneqdcseEDITLSMKELGMERA---KLHGWPNTYVFTKSMGEML 248
Cdd:cd05236  152 LIEEKVYPPPADPEKL---------------------------IDILELMDDLELERAtpkLLGGHPNTYTFTKALAERL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 249 LGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAG 328
Cdd:cd05236  205 VLKERGNLPLVIVRPSIVGATLKEPFPGWIDNFNGPDGLFLAYGKGILRTMNADPNAVADIIPVDVVANALLAAAAYSGV 284
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 145339118 329 G-SGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNP 363
Cdd:cd05236  285 RkPRELEVYHCGSSDVNPFTWGEAEELINQYLKKNP 320
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
16-319 1.68e-97

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: 294.52  E-value: 1.68e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   16 VTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQnlgdeklntLLYEKVVSVPGDIA 95
Cdd:pfam07993   1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLK---------EALERIVPVAGDLS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   96 TDQLGInDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPE 175
Cdd:pfam07993  72 EPNLGL-SEEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVSTAYVNGERGGLVEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  176 KPFIMEEirnenglqldinlerelmkqrlkelneqdcseeditLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGK-HKE 254
Cdd:pfam07993 151 KPYPEGE------------------------------------DDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREaARR 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145339118  255 NLPLVIIRPTMITstlSEPFPGWIEGLR-TVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAM 319
Cdd:pfam07993 195 GLPVVIYRPSIIT---GEPKTGWINNFDfGPRGLLGGIGKGVLPSILGDPDAVLDLVPVDYVANAI 257
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
12-349 3.59e-38

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: 140.34  E-value: 3.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  12 KTILVTGATGFLAKVFVEKILRVQPNvkKLYLLVRASDNEAATKRLRtEVFEkelfkvlRQNLGDEKLNtllyEKVVSVP 91
Cdd:COG3320    1 RTVLLTGATGFLGAHLLRELLRRTDA--RVYCLVRASDEAAARERLE-ALLE-------RYGLWLELDA----SRVVVVA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  92 GDIATDQLGINDSHlRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCvKVQLLLHVSTAYVCG--EK 169
Cdd:COG3320   67 GDLTQPRLGLSEAE-FQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATG-RLKPFHYVSTIAVAGpaDR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 170 PGLIPEKPFIMEEirnenglqldinlerelmkqrlkelneqdcseeditlsmkelgmeraklhGWPNTYVFTKSMGEMLL 249
Cdd:COG3320  145 SGVFEEDDLDEGQ--------------------------------------------------GFANGYEQSKWVAEKLV 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 250 GK-HKENLPLVIIRPTMIT---STlsepfpGWIEGLRTVDSVIIAYGKgvLKCFLVDVNSVCDMIPVDMVANAmITAAAK 325
Cdd:COG3320  175 REaRERGLPVTIYRPGIVVgdsRT------GETNKDDGFYRLLKGLLR--LGAAPGLGDARLNLVPVDYVARA-IVHLSR 245
                        330       340
                 ....*....|....*....|....
gi 145339118 326 HAGGSGvhMVYHVgsSHQNPVTFG 349
Cdd:COG3320  246 QPEAAG--RTFHL--TNPQPLSLG 265
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
14-388 5.72e-24

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: 101.67  E-value: 5.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  14 ILVTGATGFLAKVFVEKILrvqPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRqnlgdeklntllyekvvsvpGD 93
Cdd:cd05263    1 VFVTGGTGFLGRHLVKRLL---ENGFKVLVLVRSESLGEAHERIEEAGLEADRVRVLE--------------------GD 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  94 IATDQLGINDSHLRERmQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCvKVQLLLHVSTAYVCGEKPGLI 173
Cdd:cd05263   58 LTQPNLGLSAAASREL-AGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARL-DIQRFHYVSTAYVAGNREGNI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 174 PEKPFIMEEirnenglqldinlerelmkqrlkelneqdcseeditlsmkelgmeraklhGWPNTYVFTKSMGEMLLGKHK 253
Cdd:cd05263  136 RETELNPGQ--------------------------------------------------NFKNPYEQSKAEAEQLVRAAA 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 254 ENLPLVIIRPTMITstlsepfpGWIEGLRTVDsviIAYGKGVLKCF---------LVDVNSVCDMIPVDMVANAmITAAA 324
Cdd:cd05263  166 TQIPLTVYRPSIVV--------GDSKTGRIEK---IDGLYELLNLLaklgrwlpmPGNKGARLNLVPVDYVADA-IVYLS 233
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145339118 325 KHAGGSGvhMVYHVGSShqNPVTFGEIHEIAVRYFtknpLRSRNGSLITVSKVRFIPTMALFSL 388
Cdd:cd05263  234 KKPEANG--QIFHLTDP--TPQTLREIADLFKSAF----LSPGLLVLLMNEPNASLPNALRRSL 289
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
13-351 8.76e-22

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: 95.41  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  13 TILVTGATGFLAKVFVEKILRvQPNVKKLYLLVRASDNEAATKRLRtevfekELFKVLRQNLGDEKLNtllyEKVVSVPG 92
Cdd:cd05235    1 TVLLTGATGFLGAYLLRELLK-RKNVSKIYCLVRAKDEEAALERLI------DNLKEYGLNLWDELEL----SRIKVVVG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  93 DIATDQLGINDSHLrERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKcVKVQLLLHVSTAYVCGekpgl 172
Cdd:cd05235   70 DLSKPNLGLSDDDY-QELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAAT-GKLKPLHFVSTLSVFS----- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 173 ipekpfimeeirnenglqldinlerelmkqrlkelNEQDCSEEDITLSMKElgmerAKLHGWPNTYVFTKSMGEMLLGK- 251
Cdd:cd05235  143 -----------------------------------AEEYNALDDEESDDML-----ESQNGLPNGYIQSKWVAEKLLREa 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 252 HKENLPLVIIRPTMITSTlSEpfpgwiEG-LRTVDSVI-IAYGKGVLKCFLVDVNSVcDMIPVDMVAnAMITAAAKHAgg 329
Cdd:cd05235  183 ANRGLPVAIIRPGNIFGD-SE------TGiGNTDDFFWrLLKGCLQLGIYPISGAPL-DLSPVDWVA-RAIVKLALNE-- 251
                        330       340
                 ....*....|....*....|..
gi 145339118 330 SGVHMVYHVGSSHqnPVTFGEI 351
Cdd:cd05235  252 SNEFSIYHLLNPP--LISLNDL 271
Sterile pfam03015
Male sterility protein; This family represents the C-terminal region of the male sterility ...
393-495 2.05e-18

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: 460779 [Multi-domain]  Cd Length: 92  Bit Score: 79.82  E-value: 2.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  393 RYKLPLQLLKLVDIIYPWRNgdkygDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEiknteKLMFDFDP 472
Cdd:pfam03015   1 LHLLPAYLLDLLLRLLGKKP-----RLVRLYKKIHKALDVLEYFTTREWKFDNDNTEKLWDSLSPED-----RKLFNFDI 70
                          90       100
                  ....*....|....*....|...
gi 145339118  473 KGINWGDYLTNiHISGLVTHVLK 495
Cdd:pfam03015  71 RSIDWDDYFEN-YILGIRKYLLK 92
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
13-358 4.75e-18

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: 85.54  E-value: 4.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   13 TILVTGATGFLAKVFVEKILRVQPNvKKLYLLVRASDNEAATKRLRtevfekELFKVLRqnLGDEKlntLLYEKVVSVPG 92
Cdd:TIGR01746   1 TVLLTGATGFLGAYLLEELLRRSTR-AKVICLVRADSEEHAMERLR------EALRSYR--LWHEN---LAMERIEVVAG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   93 DIATDQLGINDSHLrERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKcVKVQLLLHVSTAYVC--GEKP 170
Cdd:TIGR01746  69 DLSKPRLGLSDAEW-ERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAAS-GRAKPLHYVSTISVGaaIDLS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  171 GLIPEkpfimeeirnenglqldinlerelmkqrlkelneqdcsEEDItlsmkelgmeRAKLHGWPNTYVFTKSMGEMLLG 250
Cdd:TIGR01746 147 TGVTE--------------------------------------DDAT----------VTPYPGLAGGYTQSKWVAELLVR 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  251 KHKEN-LPLVIIRPTMITstlSEPFPGWIEG----LRTVDSViIAYGKgVLKCflvDVNSVcDMIPVDMVANAmITAAAK 325
Cdd:TIGR01746 179 EASDRgLPVTIVRPGRIL---GDSYTGAWNSsdilWRMVKGC-LALGA-YPQS---PELTE-DLTPVDFVARA-IVALSS 248
                         330       340       350
                  ....*....|....*....|....*....|...
gi 145339118  326 HAGGSGVHMVYHVgsSHQNPVTFGEIHEIAVRY 358
Cdd:TIGR01746 249 RPAASAGGIVFHV--VNPNPVPLDEFLEWLERA 279
FAR_C cd09071
C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, ...
392-494 2.02e-15

C-terminal domain of fatty acyl CoA reductases; C-terminal domain of fatty acyl CoA reductases, a family of SDR-like proteins. SDRs or short-chain dehydrogenases/reductases are Rossmann-fold NAD(P)H-binding proteins. Many proteins in this FAR_C family may function as fatty acyl-CoA reductases (FARs), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as the 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. The function of this C-terminal domain is unclear.


Pssm-ID: 176924 [Multi-domain]  Cd Length: 92  Bit Score: 71.43  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 392 LRYKLPLQLLKLVDIIYpwRNGDKYGDKNRKIelvMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKnteklMFDFD 471
Cdd:cd09071    1 FLHLLPAYLLDLLLRLL--GRKPRLLKLYRKI---HKLLDLLEYFTTNEWRFDNDNTRALWERLSEEDRE-----LFNFD 70
                         90       100
                 ....*....|....*....|...
gi 145339118 472 PKGINWGDYLTNiHISGLVTHVL 494
Cdd:cd09071   71 IRSIDWDDYFEN-YIPGLRKYLL 92
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-359 1.55e-13

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 71.16  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  13 TILVTGATGFLAKVFVEkilrvqpnvkklYLL-----VRASDNEAATkrlrtevfekelfkvlRQNLGDeklntllYEKV 87
Cdd:COG0451    1 RILVTGGAGFIGSHLAR------------RLLargheVVGLDRSPPG----------------AANLAA-------LPGV 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  88 VSVPGDIAtdqlgiNDSHLRERMQKeIDIVVNVAATTNFDER-YDVGLGINTFGALNVLNFAKKCvKVQLLLHVSTAYVC 166
Cdd:COG0451   46 EFVRGDLR------DPEALAAALAG-VDAVVHLAAPAGVGEEdPDETLEVNVEGTLNLLEAARAA-GVKRFVYASSSSVY 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 167 GEKPGLIPekpfimeeirnenglqldinlerelmkqrlkelneqdcseeditlsmkelgmERAKLHGWpNTYVFTKSMGE 246
Cdd:COG0451  118 GDGEGPID----------------------------------------------------EDTPLRPV-SPYGASKLAAE 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118 247 MLLGK--HKENLPLVIIRPTMITST-LSEPFPGWIEGLRTVDSVIIaYGKGvlkcflvdvNSVCDMIPVDMVANAMITAA 323
Cdd:COG0451  145 LLARAyaRRYGLPVTILRPGNVYGPgDRGVLPRLIRRALAGEPVPV-FGDG---------DQRRDFIHVDDVARAIVLAL 214
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 145339118 324 AKHAGGSGvhmVYHVGSSHqnPVTFGEIHEIAVRYF 359
Cdd:COG0451  215 EAPAAPGG---VYNVGGGE--PVTLRELAEAIAEAL 245
PRK07201 PRK07201
SDR family oxidoreductase;
13-178 7.32e-09

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 58.04  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  13 TILVTGATGFLAKVFVEKILRVQPNvKKLYLLVRASdneaatkrlrtevfEKELFKVLRQNLGDeklntllyEKVVSVPG 92
Cdd:PRK07201   2 RYFVTGGTGFIGRRLVSRLLDRRRE-ATVHVLVRRQ--------------SLSRLEALAAYWGA--------DRVVPLVG 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  93 DIATDQLGINDSHLRERMQkeIDIVVNVAATtnfderYDVGLG------INTFGALNVLNFAKKcVKVQLLLHVSTAYVC 166
Cdd:PRK07201  59 DLTEPGLGLSEADIAELGD--IDHVVHLAAI------YDLTADeeaqraANVDGTRNVVELAER-LQAATFHHVSSIAVA 129
                        170
                 ....*....|..
gi 145339118 167 GEKPGLIPEKPF 178
Cdd:PRK07201 130 GDYEGVFREDDF 141
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
11-342 1.50e-08

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


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 57.38  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118    11 NKTILVTGATGFLAKVFVEKILRVQPN-VKKLYLLVRASDNEAATKRLRTEVFEKELFKvlrqnlgDEKLNtllyeKVVS 89
Cdd:TIGR03443  971 PITVFLTGATGFLGSFILRDLLTRRSNsNFKVFAHVRAKSEEAGLERLRKTGTTYGIWD-------EEWAS-----RIEV 1038
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118    90 VPGDIATDQLGINDShLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCvKVQLLLHVSTAYVcgek 169
Cdd:TIGR03443 1039 VLGDLSKEKFGLSDE-KWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEG-KAKQFSFVSSTSA---- 1112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   170 pglipekpfimeeirnenglqLD----INLERELMKQRLKELNEQDcseeDITLSMKELGmeraklhgwpNTYVFTKSMG 245
Cdd:TIGR03443 1113 ---------------------LDteyyVNLSDELVQAGGAGIPESD----DLMGSSKGLG----------TGYGQSKWVA 1157
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   246 EMLLGKH-KENLPLVIIRPTMITSTlSEpfpgwiEGLRTVDSVIIAYGKGVLKCFLV-DVNSVCDMIPVDMVANAMITAA 323
Cdd:TIGR03443 1158 EYIIREAgKRGLRGCIVRPGYVTGD-SK------TGATNTDDFLLRMLKGCIQLGLIpNINNTVNMVPVDHVARVVVAAA 1230
                          330
                   ....*....|....*....
gi 145339118   324 AKHAGGSGVhMVYHVgSSH 342
Cdd:TIGR03443 1231 LNPPKESEL-AVAHV-TGH 1247
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
11-162 1.10e-07

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: 53.39  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  11 NKTILVTGATGFLAKVFVEKILRVQPnvKKLYLLVRasdNEAATKRLRTEvfekelfkvLRQNLGDEKLNTLLyekvvsv 90
Cdd:cd05237    2 GKTILVTGGAGSIGSELVRQILKFGP--KKLIVFDR---DENKLHELVRE---------LRSRFPHDKLRFII------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145339118  91 pGDIATDQLGINDshlreRMQKEIDIVVNVAATT-------NFDERYDVglgiNTFGALNVLNFAKKCvKVQLLLHVST 162
Cdd:cd05237   61 -GDVRDKERLRRA-----FKERGPDIVFHAAALKhvpsmedNPEEAIKT----NVLGTKNVIDAAIEN-GVEKFVCIST 128
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
13-186 1.77e-04

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


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 43.41  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  13 TILVTGATGFLAKVFVEKILrvqpnvKKLYlLVRASdneaatkrLRTEVFEKELFKVLRQNLGDEKLntllyeKVVSVPg 92
Cdd:cd05227    1 LVLVTGATGFIASHIVEQLL------KAGY-KVRGT--------VRSLSKSAKLKALLKAAGYNDRL------EFVIVD- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  93 DIAtdqlgiNDSHLRERMqKEIDIVVNVAAT---TNFDERYDVGL-GINtfGALNVLNFAKKCVKVQ-LLLHVSTAYVCG 167
Cdd:cd05227   59 DLT------APNAWDEAL-KGVDYVIHVASPfpfTGPDAEDDVIDpAVE--GTLNVLEAAKAAGSVKrVVLTSSVAAVGD 129
                        170
                 ....*....|....*....
gi 145339118 168 EKPGliPEKPFIMEEIRNE 186
Cdd:cd05227  130 PTAE--DPGKVFTEEDWND 146
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
9-146 2.20e-04

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. 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 have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 42.78  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   9 LRNKTILVTGATGFLAKVFVEKILRVQpnVKKLYLLVRasDNEAATkrlrtevfekelfkvlrqNLGDEKLNtllyeKVV 88
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHG--AKKVYAAVR--DPGSAA------------------HLVAKYGD-----KVV 53
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145339118  89 SVPGDIaTDQLGIndSHLRERMqKEIDIVVNVA----ATTNFDERYDVGL----GINTFGALNVLN 146
Cdd:cd05354   54 PLRLDV-TDPESI--KAAAAQA-KDVDVVINNAgvlkPATLLEEGALEALkqemDVNVFGLLRLAQ 115
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
12-168 2.61e-04

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: 42.92  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  12 KTILVTGATGFLAKVFVEKILRVQPNVKKLYL--LVRASDneaatkrlrtevfekelfkvlRQNLGDEKLNtllyEKVVS 89
Cdd:cd05246    1 MKILVTGGAGFIGSNFVRYLLNKYPDYKIINLdkLTYAGN---------------------LENLEDVSSS----PRYRF 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118  90 VPGDIAtdqlginDSHLRERM--QKEIDIVVNVAATTNFDERYDVGLG---INTFGALNVLNFAKKCvKVQLLLHVSTAY 164
Cdd:cd05246   56 VKGDIC-------DAELVDRLfeEEKIDAVIHFAAESHVDRSISDPEPfirTNVLGTYTLLEAARKY-GVKRFVHISTDE 127

                 ....
gi 145339118 165 VCGE 168
Cdd:cd05246  128 VYGD 131
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
14-162 3.04e-04

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: 42.50  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339118   14 ILVTGATGFLAKVFVEKILRVQPnvKKLYLLVRAsdneaatkrlrtevfEKELFKVlRQNLGDEKLNTLLYEKVVSVPGD 93
Cdd:pfam02719   1 VLVTGGGGSIGSELCRQILKFNP--KKIILFSRD---------------ELKLYEI-RQELREKFNDPKLRFFIVPVIGD 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145339118   94 IAtdqlgiNDSHLRERMQK-EIDIVVNVAATT-------NFDErydvglGI--NTFGALNVLNFAKKCvKVQLLLHVST 162
Cdd:pfam02719  63 VR------DRERLERAMEQyGVDVVFHAAAYKhvplveyNPME------AIktNVLGTENVADAAIEA-GVKKFVLIST 128
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
115-176 2.62e-03

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 39.95  E-value: 2.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145339118  115 DIVVNVAATTNFD---ERYDVGLGINtfgALNVLNFAKKCVKVQ-LLLHVSTAYVC-GEKPGLIPEK 176
Cdd:pfam04321  51 DVVVNAAAYTAVDkaeSEPDLAYAIN---ALAPANLAEACAAVGaPLIHISTDYVFdGTKPRPYEED 114
 
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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