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Conserved domains on  [gi|767953485|ref|XP_011515548|]
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squalene monooxygenase isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 219-490 1.86e-156

Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.


:

Pssm-ID: 400679  Cd Length: 276  Bit Score: 446.39  E-value: 1.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  219 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGE-MPR- 296
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  297 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 373
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  374 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767953485  454 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 490
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PRK07045 super family cl31373
putative monooxygenase; Reviewed
 64-369 3.06e-15

putative monooxygenase; Reviewed


The actual alignment was detected with superfamily member PRK07045:

Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.64  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 142
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 211
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 212 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 287
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 288 V-----DIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 362
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 767953485 363 MTVAFKD 369
Cdd:PRK07045 305 MNLAIED 311
 
Name Accession Description Interval E-value
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 219-490 1.86e-156

Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.


Pssm-ID: 400679  Cd Length: 276  Bit Score: 446.39  E-value: 1.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  219 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGE-MPR- 296
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  297 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 373
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  374 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767953485  454 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 490
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 65-514 9.68e-131

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 391.52  E-value: 9.68e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 143
Cdd:PTZ00367  33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 144 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 214
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 215 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 275
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 276 IYQISSSETRVLVDIRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 351
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 352 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 422
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 423 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 482
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499

                        490       500       510
                 ....*....|....*....|....*....|..
gi 767953485 483 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 514
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 63-432 2.75e-23

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 100.40  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 142
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 221
Cdd:COG0654   80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDIRGEmprnlrey 301
Cdd:COG0654  151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 302 mVEKIYPQIPDHLKEpFLEATDNSHLRSmpASFLPPSSVKKRgVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 379
Cdd:COG0654  188 -LRARLAAAGPRLGE-LLELSPRSAFPL--RRRRAERWRRGR-VVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 380 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 432
Cdd:COG0654  262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
PRK07045 PRK07045
putative monooxygenase; Reviewed
 64-369 3.06e-15

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.64  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 142
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 211
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 212 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 287
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 288 V-----DIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 362
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 767953485 363 MTVAFKD 369
Cdd:PRK07045 305 MNLAIED 311
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
68-97 2.23e-06

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 49.90  E-value: 2.23e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG0665    5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 67-233 2.65e-06

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 49.32  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 106
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  107 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 180
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767953485  181 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 233
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 67-430 1.52e-05

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 47.44  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   67 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 129
Cdd:TIGR01989   2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  130 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 203
Cdd:TIGR01989  81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  204 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 258
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  259 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDIRGEMPR-NLREYMVEKIY 307
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  308 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 377
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767953485  378 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 430
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 64-113 8.28e-03

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad 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 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 (15-PGDH) numbering). 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) 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 ketoacyl reductases 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: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 38.21  E-value: 8.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG 54
 
Name Accession Description Interval E-value
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 219-490 1.86e-156

Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.


Pssm-ID: 400679  Cd Length: 276  Bit Score: 446.39  E-value: 1.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  219 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGE-MPR- 296
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  297 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 373
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  374 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767953485  454 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 490
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 65-514 9.68e-131

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 391.52  E-value: 9.68e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 143
Cdd:PTZ00367  33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 144 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 214
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 215 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 275
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 276 IYQISSSETRVLVDIRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 351
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 352 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 422
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 423 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 482
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499

                        490       500       510
                 ....*....|....*....|....*....|..
gi 767953485 483 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 514
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
PLN02985 PLN02985
squalene monooxygenase
 67-473 3.08e-106

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 326.86  E-value: 3.08e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHdqESKS 146
Cdd:PLN02985  45 DVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVY--KDGK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 147 EVQIPYPLSENN--QVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELhAPLTV 224
Cdd:PLN02985 123 EAVAPFPVDNNNfpYEPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTAL-APLTV 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 225 VADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDI---------RGEMP 295
Cdd:PLN02985 202 VCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTMLYQISSTDVRCVFEVlpdnipsiaNGEMS 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 296 rnlrEYMVEKIYPQIPDHLKEPFLEATDN-SHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWR 374
Cdd:PLN02985 282 ----TFVKNTIAPQVPPKLRKIFLKGIDEgAHIKVVPTKRMSATLSDKKGVIVLGDAFNMRHPAIASGMMVLLSDILILR 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 375 KLLKGIPDLYDDAAIFEAKKSFYWARKtSHSFVVNILAQALYE-LFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 453
Cdd:PLN02985 358 RLLQPLSNLGNANKVSEVIKSFYDIRK-PMSATVNTLGNAFSQvLVASTDEAKEAMRQGCYDYLCSGGFRTSGMMALLGG 436

                        410       420
                 ....*....|....*....|
gi 767953485 454 LSPNPLVLIGHFFAVAIYAV 473
Cdd:PLN02985 437 MNPRPLSLIYHLCAITLSSI 456
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 63-432 2.75e-23

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 100.40  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 142
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 221
Cdd:COG0654   80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDIRGEmprnlrey 301
Cdd:COG0654  151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 302 mVEKIYPQIPDHLKEpFLEATDNSHLRSmpASFLPPSSVKKRgVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 379
Cdd:COG0654  188 -LRARLAAAGPRLGE-LLELSPRSAFPL--RRRRAERWRRGR-VVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767953485 380 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 432
Cdd:COG0654  262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
73-368 1.32e-17

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 83.09  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  73 AGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEgldaQVVNGYMIHDQeSKSEVQIPY 152
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSP-GGKSVELPP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 153 PLSENNQVQsgRAfhhgRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMgVqykdkETGDIKELHAPLTVVADGLFS 231
Cdd:COG0644   76 GRGGGYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 232 KFRKSLVSNKVSVSSHFVGFLMKnapqfkanhaelilanpspvliyqissseTRVLVDIRGEMPRNLREYMVEKIYPQ-- 309
Cdd:COG0644  143 LLARKLGLKRRSDEPQDYALAIK-----------------------------EHWELPPLEGVDPGAVEFFFGEGAPGgy 193

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953485 310 ---IPdhlkepfleATDNSHLRSMPASFLPPSSVkKRGVLLLGDAYNMRHPLTGGGMTVAFK 368
Cdd:COG0644  194 gwvFP---------LGDGRVSVGIPLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIHLAMK 245
PRK07045 PRK07045
putative monooxygenase; Reviewed
 64-369 3.06e-15

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.64  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 142
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 211
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 212 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 287
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 288 V-----DIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 362
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 767953485 363 MTVAFKD 369
Cdd:PRK07045 305 MNLAIED 311
PRK06185 PRK06185
FAD-dependent oxidoreductase;
67-236 6.96e-13

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 70.27  E-value: 6.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIE------RDLKepdrivGEFLQPGGYHVLKDLGLGDTVEGLDaqvvngymiH 140
Cdd:PRK06185   8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDFR------GDTVHPSTLELMDELGLLERFLELP---------H 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSEVQIPyplseNNQVQS---GRAFHHGRFIM---------SLRKAAMAEPNAKFIEGV-VLQLLEEDDVVMGVQY 207
Cdd:PRK06185  73 QKVRTLRFEIG-----GRTVTLadfSRLPTPYPYIAmmpqwdfldFLAEEASAYPNFTLRMGAeVTGLIEEGGRVTGVRA 147

                        170       180
                 ....*....|....*....|....*....
gi 767953485 208 KDKEtGDIkELHAPLTVVADGLFSKFRKS 236
Cdd:PRK06185 148 RTPD-GPG-EIRADLVVGADGRHSRVRAL 174
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
62-249 6.19e-12

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 67.37  E-value: 6.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIErdlkEPDRIvGEF-----LQPGGYHVLKDLGLGDTVEGLdaQVVNG 136
Cdd:PRK08163   1 MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLE----QAAEI-GEIgagiqLGPNAFSALDALGVGEAARQR--AVFTD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 137 YMI-HDQESKSEV-QIPyplsennqvqSGRAF-----------HHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDD--V 201
Cdd:PRK08163  74 HLTmMDAVDAEEVvRIP----------TGQAFrarfgnpyaviHRADIHLSLLEAVLDHPLVEFRTSTHVVGIEQDGdgV 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767953485 202 VMGVQYKDKETGDIkelhaplTVVADGLFSKFRKSLVSNKVSVSSHFV 249
Cdd:PRK08163 144 TVFDQQGNRWTGDA-------LIGCDGVKSVVRQSLVGDAPRVTGHVV 184
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 65-369 3.66e-11

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 64.65  E-value: 3.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   65 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIV---GEFLQPGGYHVLKDLGLGDTVegLDAQVVNGYMIHd 141
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERH---ATTSVlprAHGLNQRTMELLRQAGLEDRI--LAEGVPHEGMGL- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  142 qesksEVQIPYPLSENNQVQSGRAFH---HGRFIMSLRKAAMAEPnAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKEL 218
Cdd:pfam01494  75 -----AFYNTRRRADLDFLTSPPRVTvypQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRDRRDGEEYTV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  219 HAPLTVVADGLFSKFRKSL---VSNKVSVSSHFVG--FLMKNAPQFKANHA--ELILANPSPVLIYQISSSETR---VLV 288
Cdd:pfam01494 149 RAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDvlFDAPDLSDPVERAFvhYLIYAPHSRGFMVGPWRSAGReryYVQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  289 DIRGEMPRNLREymvekiyPQIPDHLKEPFLEAT--DNSHLRSMPASFLPpssVKKR--------GVLLLGDAYNmRHPL 358
Cdd:pfam01494 229 VPWDEEVEERPE-------EFTDEELKQRLRSIVgiDLALVEILWKSIWG---VASRvatryrkgRVFLAGDAAH-IHPP 297

                         330
                  ....*....|..
gi 767953485  359 TGG-GMTVAFKD 369
Cdd:pfam01494 298 TGGqGLNTAIQD 309
PRK09126 PRK09126
FAD-dependent hydroxylase;
68-237 1.98e-06

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 49.94  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD----LKEPD---RIVGefLQPGGYHVLKDLGLGDTVEG------LDAQVV 134
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQplaaLADPAfdgREIA--LTHASREILQRLGAWDRIPEdeisplRDAKVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 135 NG---YMIH-DQESKSEVQIPYpLSENNQVQsgRAfhhgrfimsLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDK 210
Cdd:PRK09126  84 NGrspFALTfDARGRGADALGY-LVPNHLIR--RA---------AYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANG 151

                        170       180
                 ....*....|....*....|....*..
gi 767953485 211 ETgdikeLHAPLTVVADGLFSKFRKSL 237
Cdd:PRK09126 152 RR-----LTARLLVAADSRFSATRRQL 173
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
68-97 2.23e-06

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 49.90  E-value: 2.23e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG0665    5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 67-233 2.65e-06

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 49.32  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 106
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  107 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 180
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767953485  181 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 233
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
PRK06847 PRK06847
hypothetical protein; Provisional
 68-363 4.20e-06

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 49.10  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTV-------EGLDAQVVNGYMIH 140
Cdd:PRK06847   7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECleagfgfDGVDLFDPDGTLLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSEVQIPYPlsenNQVQSGR-AFHHgrfImsLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETGdikelH 219
Cdd:PRK06847  87 ELPTPRLAGDDLP----GGGGIMRpALAR---I--LADAARAA-GADVRLGTTVTAIEQDDDGVTVTFSDGTTG-----R 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 220 APLTVVADGLFSKFRKSLVSNK--------------VSVSSHFVGFLMKNAPQFKANhaelilANP-SPVLIYQ--ISSS 282
Cdd:PRK06847 152 YDLVVGADGLYSKVRSLVFPDEpepeytgqgvwravLPRPAEVDRSLMYLGPTTKAG------VVPlSEDLMYLfvTEPR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 283 ETRVLVDiRGEMPRNLREYMVEKIYPQIPDhLKEPfleATDNSHL--RSMPASFLPPSSVKKRgVLLLGDAYnmrHPLT- 359
Cdd:PRK06847 226 PDNPRIE-PDTLAALLRELLAPFGGPVLQE-LREQ---ITDDAQVvyRPLETLLVPAPWHRGR-VVLIGDAA---HATTp 296


                 ....*...
gi 767953485 360 ----GGGM 363
Cdd:PRK06847 297 hlaqGAGM 304
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 68-125 7.93e-06

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 47.75  E-value: 7.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHV----------LKDLGLGDT 125
Cdd:COG0569   98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD---PERV--ERLAEEDVLVivgdatdeevLEEAGIEDA 160
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 67-430 1.52e-05

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 47.44  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   67 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 129
Cdd:TIGR01989   2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  130 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 203
Cdd:TIGR01989  81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  204 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 258
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  259 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDIRGEMPR-NLREYMVEKIY 307
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  308 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 377
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767953485  378 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 430
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
62-102 3.48e-05

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 46.29  E-value: 3.48e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767953485  62 SQNDPEVIIVGAGVLGSALAAVLSR-DGRKVTVIErdlKEPD 102
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALARELSRyEDLKVLVLE---KEDD 39
trkA PRK09496
Trk system potassium transporter TrkA;
68-136 3.63e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 46.27  E-value: 3.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQpggyhvlkdlglgdtvEGLDAQVVNG 136
Cdd:PRK09496   3 IIIVGAGQVGYTLAENLSGENNDVTVIDTD---EERL--RRLQ----------------DRLDVRTVVG 50
PRK07588 PRK07588
FAD-binding domain;
68-250 5.58e-05

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 45.50  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIER--DLKEPDRIVgEFLQPgGYHVLKDLGLGDTVEGLDAQVVNgymIHDQESK 145
Cdd:PRK07588   3 VAISGAGIAGPTLAYWLRRYGHEPTLIERapELRTGGYMV-DFWGV-GYEVAKRMGITDQLREAGYQIEH---VRSVDPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 146 SEVqipyplSENNQVQSGRAFHHGRFImSLRKAAMAEPNAKFIEGVVLQLL---------EEDDVVMGVQYKDKETGDik 216
Cdd:PRK07588  78 GRR------KADLNVDSFRRMVGDDFT-SLPRGDLAAAIYTAIDGQVETIFddsiatideHRDGVRVTFERGTPRDFD-- 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767953485 217 elhapLTVVADGLFSKFRkSLVSNKVSVSSHFVG 250
Cdd:PRK07588 149 -----LVIGADGLHSHVR-RLVFGPERDFEHYLG 176
PRK07233 PRK07233
hypothetical protein; Provisional
 70-136 7.05e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 45.26  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  70 IVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVG-----EFlqpGG------YH-----------VLKDLGLGDTV- 126
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEAD----DQLGGlaasfEF---GGlpierfYHhifksdealleLLDELGLEDKLr 76

                         90
                 ....*....|..
gi 767953485 127 --EGLDAQVVNG 136
Cdd:PRK07233  77 wrETKTGYYVDG 88
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 68-132 9.04e-05

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 44.42  E-value: 9.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyHVLKDLG----LGDTVEGLDAQ 132
Cdd:COG0446  127 AVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLE----EELREHGvelrLGETVVAIDGD 194
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
70-96 9.23e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.59  E-value: 9.23e-05
                          10        20
                  ....*....|....*....|....*..
gi 767953485   70 IVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
PRK06184 PRK06184
hypothetical protein; Provisional
 63-155 1.09e-04

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 44.59  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  63 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERdLKEP---DRivGEFLQPGGYHVLKDLGLGDTVEGL---------- 129
Cdd:PRK06184   1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEK-APEPfpgSR--GKGIQPRTQEVFDDLGVLDRVVAAgglyppmriy 77

                         90       100
                 ....*....|....*....|....*...
gi 767953485 130 --DAQVVNGYMIHDQESKSEvqIPYPLS 155
Cdd:PRK06184  78 rdDGSVAESDMFAHLEPTPD--EPYPLP 103
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 62-235 1.74e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 43.82  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDL-------KEPD-RIVGefLQPGGYHVLKDLGLGDTVEGL---- 129
Cdd:PRK08020   2 TNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAApapfdadSQPDvRISA--ISAASVALLKGLGVWDAVQAMrshp 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 130 ----------DAQVVN----------GYMIhdqesksevqipyplsENNQVQsgrafhhgrfiMSLRKAAMAEPNAKFIE 189
Cdd:PRK08020  80 yrrletweweTAHVVFdaaelklpelGYMV----------------ENRVLQ-----------LALWQALEAHPNVTLRC 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767953485 190 GVVLQLLEEDDVVMGVQYKDKEtgdikELHAPLTVVADGLFSKFRK 235
Cdd:PRK08020 133 PASLQALQRDDDGWELTLADGE-----EIQAKLVIGADGANSQVRQ 173
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 67-97 1.98e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 44.07  E-value: 1.98e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
58-237 2.15e-04

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 43.74  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  58 TSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGeflQPGGYH-------VLKDLGLGDTVeGLD 130
Cdd:PRK06183   3 AQHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW----PTLYD---LPRAVGiddealrVLQAIGLADEV-LPH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 131 AQVVNGYMIHDQESKSEVQIPYPlsennqvqSGRafHHG---RFIMS-------LRKAAMAEPNAKFIEGV-VLQLLEED 199
Cdd:PRK06183  75 TTPNHGMRFLDAKGRCLAEIARP--------STG--EFGwprRNAFHqplleavLRAGLARFPHVRVRFGHeVTALTQDD 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767953485 200 DVVMgVQYKDkETGDIKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK06183 145 DGVT-VTLTD-ADGQRETVRARYVVGCDGANSFVRRTL 180
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 68-110 2.83e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 39.49  E-value: 2.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767953485   68 VIIVGAGVLGSALAAVLSRDGRKVTVIER---DLKEPDRIVGEFLQ 110
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERrdrLLPGFDPEIAKILQ 47
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 68-117 3.00e-04

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


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 40.59  E-value: 3.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767953485   68 VIIVGAGVLGSALAAVLSRDGrKVTVIERDlkePDRIvgEFLQPGGYHVL 117
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKD---EERV--EELREEGVPVV 44
PRK07538 PRK07538
hypothetical protein; Provisional
 68-237 3.85e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 42.96  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIE--RDLKEPDriVGEFLQPGGYHVLKDLGLGDTvegLDAQVVNGYMI-----H 140
Cdd:PRK07538   3 VLIAGGGIGGLTLALTLHQRGIEVVVFEaaPELRPLG--VGINLLPHAVRELAELGLLDA---LDAIGIRTRELayfnrH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESKSE---VQIPYPLSennQVqsgrAFHHGRFIMSLRKAAMAEPNAKFIE---GVVLQLLEEDDVVMGVQykDKETGD 214
Cdd:PRK07538  78 GQRIWSEprgLAAGYDWP---QY----SIHRGELQMLLLDAVRERLGPDAVRtghRVVGFEQDADVTVVFLG--DRAGGD 148

                        170       180
                 ....*....|....*....|...
gi 767953485 215 IKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK07538 149 LVSVRGDVLIGADGIHSAVRAQL 171
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 68-113 4.01e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 42.19  E-value: 4.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:PRK08277  14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 68-96 6.37e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 42.51  E-value: 6.37e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRD-GRKVTVIER 96
Cdd:COG2303    7 YVIVGAGSAGCVLANRLSEDaGLRVLLLEA 36
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 68-121 6.74e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 41.92  E-value: 6.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485   68 VIIVGAGVLGSALAAVLSRDGRKVTVIE---RDLKEPDRIVGEFLQpggyHVLKDLG 121
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEaldRLLRAFDEEISAALE----KALEKNG 207
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 67-250 7.37e-04

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 41.82  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIV--GEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIhdqeS 144
Cdd:PRK10157   7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVtgGRLYAHSLEHIIPGFADSAPVERLITHEKLAFMT----E 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 145 KSEVQIPYpLSENNQVQSGRAFH--HGRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMGVQykdkETGDIKElhAP 221
Cdd:PRK10157  83 KSAMTMDY-CNGDETSPSQRSYSvlRSKFDAWLMEQA-EEAGAQLITGIrVDNLVQRDGKVVGVE----ADGDVIE--AK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 767953485 222 LTVVADGLFSKFRKSL-VSNKVSVSSHFVG 250
Cdd:PRK10157 155 TVILADGVNSILAEKLgMAKRVKPTDVAVG 184
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 68-96 8.43e-04

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 41.76  E-value: 8.43e-04
                         10        20
                 ....*....|....*....|....*....
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG1233    6 VVVIGAGIGGLAAAALLARAGYRVTVLEK 34
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
68-117 9.19e-04

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 41.25  E-value: 9.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHVL 117
Cdd:COG1226  127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLD---PERV--EELRRFGIKVY 171
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
68-130 1.06e-03

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 41.28  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQpggyHVLKDLG----LGDTVEGLD 130
Cdd:COG1251  145 VVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLlprqldeeAGALLQ----RLLEALGvevrLGTGVTEIE 211
PRK00711 PRK00711
D-amino acid dehydrogenase;
67-96 1.07e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 41.32  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 68-108 1.54e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.93  E-value: 1.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIVGEF 108
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSRLGVKVTVFER----GDRILPLE 208
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 70-126 1.81e-03

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 40.61  E-value: 1.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485  70 IVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIvgEFLQPGGYHVLKDLGLGDTV 126
Cdd:COG1893    5 ILGAGAIGGLLGARLARAGHDVTLVAR----GAHA--EALRENGLRLESPDGDRTTV 55
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
62-97 2.36e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 40.55  E-value: 2.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767953485  62 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERD 97
Cdd:COG3573    2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQE 37
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 66-108 2.51e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 40.46  E-value: 2.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767953485  66 PE-VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGEF 108
Cdd:COG1249  168 PKsLVVIGGGYIGLEFAQIFARLGSEVTLVERG----DRLLPGE 207
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
68-235 3.64e-03

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 39.58  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  68 VIIVGAGVLGSALAAVLsRDGR---KVTVIERDLKEP--DRIVGEFLQPGGYHVLKDLGLGDTVEGlDAQVVNGYMIHDQ 142
Cdd:PRK07333   4 VVIAGGGYVGLALAVAL-KQAAphlPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAP-EAQPITDMVITDS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 143 ESKSEVQiPYPLSENNQVQSGRAFHH----GRFIMSLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeL 218
Cdd:PRK07333  82 RTSDPVR-PVFLTFEGEVEPGEPFAHmvenRVLINALRKRAEAL-GIDLREATSVTDFETRDEGVTVTLSDGSV-----L 154

                        170
                 ....*....|....*..
gi 767953485 219 HAPLTVVADGLFSKFRK 235
Cdd:PRK07333 155 EARLLVAADGARSKLRE 171
PRK07364 PRK07364
FAD-dependent hydroxylase;
58-95 4.03e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 39.62  E-value: 4.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767953485  58 TSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE 95
Cdd:PRK07364  11 LPSTRSLTYDVAIVGGGIVGLTLAAALKDSGLRIALIE 48
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 67-237 4.50e-03

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 39.37  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485  67 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKE------PDRIVGEfLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH 140
Cdd:PRK08850   6 DVAIIGGGMVGLALAAALKESDLRIAVIEGQLPEealnelPDVRVSA-LSRSSEHILRNLGAWQGIEARRAAPYIAMEVW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485 141 DQESksevqipyplsennqvqsgraFHHGRFimslRKAAMAEPN-AKFIEGVVLQL------LEEDDVVM-------GVQ 206
Cdd:PRK08850  85 EQDS---------------------FARIEF----DAESMAQPDlGHIVENRVIQLalleqvQKQDNVTLlmparcqSIA 139

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767953485 207 YKDKET----GDIKELHAPLTVVADGLFSKFRKSL 237
Cdd:PRK08850 140 VGESEAwltlDNGQALTAKLVVGADGANSWLRRQM 174
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
66-96 4.52e-03

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 39.09  E-value: 4.52e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767953485  66 PEVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEK 34
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 64-97 4.60e-03

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 39.21  E-value: 4.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERD 97
Cdd:PRK07688  23 REKHVLIIGAGALGTANAEMLVRAGvGKVTIVDRD 57
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 68-105 5.34e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 36.80  E-value: 5.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 767953485   68 VIIVGAGVLGSALAAVLSRDG--RKVTVIERDLKEPDRIV 105
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALA 40
PRK06370 PRK06370
FAD-containing oxidoreductase;
69-98 5.71e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 39.03  E-value: 5.71e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 767953485  69 IIVGAGVLGSALAAVLSRDGRKVTVIERDL 98
Cdd:PRK06370   9 IVIGAGQAGPPLAARAAGLGMKVALIERGL 38
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 43-95 5.91e-03

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 39.14  E-value: 5.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767953485  43 GTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE 95
Cdd:PRK09754 122 GERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIE 174
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 66-124 6.15e-03

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 39.05  E-value: 6.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953485  66 PEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQPGGYHV-----------LKDLGLGD 124
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS----DRVgglirtveVDGFRIDRGPHSfltrdpevlelLRELGLGD 75
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 67-205 6.35e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 38.22  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953485   67 EVIIVGAGVLGSALAAVLSRD-GRKVTVIERDLkepdrivgeflQPGGyhvlkdlGLGdtvegLDAQVVNgYMIHDQESK 145
Cdd:pfam01946  19 DVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSV-----------SPGG-------GAW-----LGGQLFS-AMVVRKPAH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767953485  146 ---SEVQIPYPLSENNQVQSgrafHHGRFIMSLRKAAMAEPNAKFIEGVVLQ--LLEEDDVVMGV 205
Cdd:pfam01946  75 lflDEFGIPYEDEGDYVVVK----HAALFTSTLMSKALQLPNVKLFNATSVEdlIVRPGVGVAGV 135
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
59-131 6.41e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 39.12  E-value: 6.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953485  59 STSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPgGYHVLKDLGLGDTVEGLDA 131
Cdd:PRK07494   1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGP-SIRFLERLGLWARLAPHAA 72
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 60-96 6.81e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 39.08  E-value: 6.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767953485  60 TSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIER 96
Cdd:COG2072    1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
68-130 6.87e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 38.74  E-value: 6.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767953485  68 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLG----LGDTVEGLD 130
Cdd:PRK04965 144 VLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGvhllLKSQLQGLE 210
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
60-97 7.22e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 38.75  E-value: 7.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767953485  60 TSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE-RD 97
Cdd:COG1231    2 SRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD 40
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 65-100 8.22e-03

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 38.56  E-value: 8.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767953485  65 DPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERDLKE 100
Cdd:PRK12475  24 EKHVLIVGAGALGAANAEALVRAGiGKLTIADRDYVE 60
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 64-113 8.28e-03

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad 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 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 (15-PGDH) numbering). 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) 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 ketoacyl reductases 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: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 38.21  E-value: 8.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767953485  64 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 113
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG 54
 
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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