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Conserved domains on  [gi|675758812|ref|XP_008972170|]
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squalene monooxygenase isoform X2 [Pan paniscus]

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 ...
 218-489 3.35e-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: 445.62  E-value: 3.35e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  218 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDVRGE-MPR- 295
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  296 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 372
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  373 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 452
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 675758812  453 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 489
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PRK07045 super family cl31373
putative monooxygenase; Reviewed
 63-368 3.63e-15

putative monooxygenase; Reviewed


The actual alignment was detected with superfamily member PRK07045:

Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.25  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 141
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 210
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 211 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 286
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 287 V-----DVRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 361
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 675758812 362 MTVAFKD 368
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 ...
 218-489 3.35e-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: 445.62  E-value: 3.35e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  218 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDVRGE-MPR- 295
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  296 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 372
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  373 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 452
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 675758812  453 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 489
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 64-513 2.85e-130

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 390.37  E-value: 2.85e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  64 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 142
Cdd:PTZ00367  33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 143 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 213
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 214 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 274
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 275 IYQISSSETRVLVDVRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 350
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 351 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 421
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 422 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 481
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499

                        490       500       510
                 ....*....|....*....|....*....|..
gi 675758812 482 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 513
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 62-431 2.64e-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: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  62 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 141
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 220
Cdd:COG0654   80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 221 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDVRGEmprnlrey 300
Cdd:COG0654  151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 301 mVEKIYPQIPDHLKEpFLEATDNSHLrsmPASFLPPSSVKKRGVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 378
Cdd:COG0654  188 -LRARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 675758812 379 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 431
Cdd:COG0654  262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
PRK07045 PRK07045
putative monooxygenase; Reviewed
 63-368 3.63e-15

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.25  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 141
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 210
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 211 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 286
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 287 V-----DVRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 361
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 675758812 362 MTVAFKD 368
Cdd:PRK07045 305 MNLAIED 311
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
67-96 2.22e-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: 2.22e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 96
Cdd:COG0665    5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 66-232 3.36e-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: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  106 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 179
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 675758812  180 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 232
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 66-429 1.45e-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: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   66 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 128
Cdd:TIGR01989   2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  129 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 202
Cdd:TIGR01989  81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  203 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 257
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  258 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDVRGEMPR-NLREYMVEKIY 306
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  307 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 376
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 675758812  377 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 429
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 63-112 8.26e-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: 8.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 112
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 ...
 218-489 3.35e-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: 445.62  E-value: 3.35e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  218 HAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDVRGE-MPR- 295
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  296 ---NLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLW 372
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  373 RKLLKGIPDLYDDAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 452
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 675758812  453 LSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALL 489
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 64-513 2.85e-130

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 390.37  E-value: 2.85e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  64 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVvNGYMIHDQE 142
Cdd:PTZ00367  33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 143 SKsEVQIPYplsenNQVQSGRAFHHGRFIMSLRKAAMA--EPNAKFIEGVVLQLLEED----DVVMGVQYKDKETGD--- 213
Cdd:PTZ00367 112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDvpe 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 214 -----------------IKELHAPLTVVADGLFSKFRKSLVSNKVSVS--SHFVGFLMKNAPQFKANHAELILANPSPVL 274
Cdd:PTZ00367 186 npfredppsanpsattvRKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 275 IYQISSSETRVLVDVRGEMPRNLRE---YMVEKIYPQIPDHLKEPFLEAT-DNSHLRSMPASFLPPSSVKKRGVLLLGDA 350
Cdd:PTZ00367 266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASkDTKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 351 YNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYD---------DAAIFEAKKSFYWARKTsHSFVVNILAQALYELFSAT 421
Cdd:PTZ00367 346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 422 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV--------------------YFCFKSEPW 481
Cdd:PTZ00367 425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVlnlimetgaysifgkqlssfEKLTNVASF 499

                        490       500       510
                 ....*....|....*....|....*....|..
gi 675758812 482 ITKPRALLSSGAVLYKACSVIFPLIYSEMKYM 513
Cdd:PTZ00367 500 FVDPERIKHALYLLGAATTIAAPLAKSEFVSL 531
PLN02985 PLN02985
squalene monooxygenase
 39-472 1.04e-106

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 328.01  E-value: 1.04e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  39 RRRKGTNISEtsligaAACTSTSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKD 118
Cdd:PLN02985  24 RKKKATELAD------AVAEERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERMMGEFMQPGGRFMLSK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 119 LGLGDTVEGLDAQVVNGYMIHdqESKSEVQIPYPLSENN--QVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLE 196
Cdd:PLN02985  98 LGLEDCLEGIDAQKATGMAVY--KDGKEAVAPFPVDNNNfpYEPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 197 EDDVVMGVQYKDKETGDIKELhAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIY 276
Cdd:PLN02985 176 EKGVIKGVTYKNSAGEETTAL-APLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTMLY 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 277 QISSSETRVLVDV---------RGEMPrnlrEYMVEKIYPQIPDHLKEPFLEATDN-SHLRSMPASFLPPSSVKKRGVLL 346
Cdd:PLN02985 255 QISSTDVRCVFEVlpdnipsiaNGEMS----TFVKNTIAPQVPPKLRKIFLKGIDEgAHIKVVPTKRMSATLSDKKGVIV 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 347 LGDAYNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKtSHSFVVNILAQALYE-LFSATDDSL 425
Cdd:PLN02985 331 LGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRK-PMSATVNTLGNAFSQvLVASTDEAK 409

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 675758812 426 HQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAV 472
Cdd:PLN02985 410 EAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITLSSI 456
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 62-431 2.64e-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: 2.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  62 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLdAQVVNGYMIHDQ 141
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 ESKSEV-QIPYPLSennQVQSGRAFHHGRFIMSLRKAAmAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeLHAP 220
Cdd:COG0654   80 SDGRVLaRFDAAET---GLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 221 LTVVADGLFSKFRKSLvsnkvsvsshFVGFLMKNAPQfkanhaelilanpspvliyqissseTRVLVDVRGEmprnlrey 300
Cdd:COG0654  151 LVVGADGARSAVRRLL----------GIGFTGRDYPQ-------------------------RALWAGVRTE-------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 301 mVEKIYPQIPDHLKEpFLEATDNSHLrsmPASFLPPSSVKKRGVLLLGDA-YNMrHPLTGGGMTVAFKDIK-LWRKLLKG 378
Cdd:COG0654  188 -LRARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDAAaLAWKLAAA 261

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 675758812 379 IPDLYDDAAI--FEAkksfywARKTSHSFVVNiLAQALYELFSATDDSLHQLRKA 431
Cdd:COG0654  262 LRGRDDEAALarYER------ERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
72-367 1.05e-17

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 83.48  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  72 AGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEgldaQVVNGYMIHDQeSKSEVQIPY 151
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSP-GGKSVELPP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 152 PLSENNQVQsgRAfhhgRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMgVqykdkETGDIKELHAPLTVVADGLFS 230
Cdd:COG0644   76 GRGGGYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 231 KFRKSLVSNKVSVSSHFVGFLMKnapqfkanhaelilanpspvliyqissseTRVLVDVRGEMPRNLREYMVEKIYPQ-- 308
Cdd:COG0644  143 LLARKLGLKRRSDEPQDYALAIK-----------------------------EHWELPPLEGVDPGAVEFFFGEGAPGgy 193

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675758812 309 ---IPdhlkepfleATDNSHLRSMPASFLPPSSVkKRGVLLLGDAYNMRHPLTGGGMTVAFK 367
Cdd:COG0644  194 gwvFP---------LGDGRVSVGIPLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIHLAMK 245
PRK07045 PRK07045
putative monooxygenase; Reviewed
 63-368 3.63e-15

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.25  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGY-MIHDQ 141
Cdd:PRK07045   4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 EsksevqipyPL-SENNQVQSGRAFhhgrFIM----SLRKAAMA----EPNAKFIEGVVLQLLE--EDDVVMGVQYKDKE 210
Cdd:PRK07045  84 E---------LIaSLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 211 TgdikelHAPLTVV-ADGLFSKFRKSLV---SNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVL 286
Cdd:PRK07045 151 R------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 287 V-----DVRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG 361
Cdd:PRK07045 225 VsfpadEMQGYLADTTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQG 304


                 ....*..
gi 675758812 362 MTVAFKD 368
Cdd:PRK07045 305 MNLAIED 311
PRK06185 PRK06185
FAD-dependent oxidoreductase;
66-235 8.75e-13

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 69.89  E-value: 8.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIE------RDLKepdrivGEFLQPGGYHVLKDLGLGDTVEGLDaqvvngymiH 139
Cdd:PRK06185   8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDFR------GDTVHPSTLELMDELGLLERFLELP---------H 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 140 DQESKSEVQIPyplseNNQVQS---GRAFHHGRFIM---------SLRKAAMAEPNAKFIEGV-VLQLLEEDDVVMGVQY 206
Cdd:PRK06185  73 QKVRTLRFEIG-----GRTVTLadfSRLPTPYPYIAmmpqwdfldFLAEEASAYPNFTLRMGAeVTGLIEEGGRVTGVRA 147

                        170       180
                 ....*....|....*....|....*....
gi 675758812 207 KDKEtGDIkELHAPLTVVADGLFSKFRKS 235
Cdd:PRK06185 148 RTPD-GPG-EIRADLVVGADGRHSRVRAL 174
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
61-248 6.17e-12

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 67.37  E-value: 6.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  61 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIErdlkEPDRIvGEF-----LQPGGYHVLKDLGLGDTVEGLdaQVVNG 135
Cdd:PRK08163   1 MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLE----QAAEI-GEIgagiqLGPNAFSALDALGVGEAARQR--AVFTD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 136 YMI-HDQESKSEV-QIPyplsennqvqSGRAF-----------HHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDD--V 200
Cdd:PRK08163  74 HLTmMDAVDAEEVvRIP----------TGQAFrarfgnpyaviHRADIHLSLLEAVLDHPLVEFRTSTHVVGIEQDGdgV 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 675758812 201 VMGVQYKDKETGDIkelhaplTVVADGLFSKFRKSLVSNKVSVSSHFV 248
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.
 64-368 5.68e-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: 63.88  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   64 DPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIV---GEFLQPGGYHVLKDLGLGDTVegLDAQVVNGYMIHd 140
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERH---ATTSVlprAHGLNQRTMELLRQAGLEDRI--LAEGVPHEGMGL- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  141 qesksEVQIPYPLSENNQVQSGRAFH---HGRFIMSLRKAAMAEPnAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKEL 217
Cdd:pfam01494  75 -----AFYNTRRRADLDFLTSPPRVTvypQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRDRRDGEEYTV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  218 HAPLTVVADGLFSKFRKSL---VSNKVSVSSHFVG--FLMKNAPQFKANHA--ELILANPSPVLIYQISSSETR---VLV 287
Cdd:pfam01494 149 RAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDvlFDAPDLSDPVERAFvhYLIYAPHSRGFMVGPWRSAGReryYVQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  288 DVRGEMPRNLREymvekiyPQIPDHLKEPFLEAT--DNSHLRSMPASFLPpssVKKR--------GVLLLGDAYNmRHPL 357
Cdd:pfam01494 229 VPWDEEVEERPE-------EFTDEELKQRLRSIVgiDLALVEILWKSIWG---VASRvatryrkgRVFLAGDAAH-IHPP 297

                         330
                  ....*....|..
gi 675758812  358 TGG-GMTVAFKD 368
Cdd:pfam01494 298 TGGqGLNTAIQD 309
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
67-96 2.22e-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: 2.22e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERD 96
Cdd:COG0665    5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
PRK09126 PRK09126
FAD-dependent hydroxylase;
67-236 2.25e-06

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 49.94  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERD----LKEPD---RIVGefLQPGGYHVLKDLGLGDTVEG------LDAQVV 133
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQplaaLADPAfdgREIA--LTHASREILQRLGAWDRIPEdeisplRDAKVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 134 NG---YMIH-DQESKSEVQIPYpLSENNQVQsgRAfhhgrfimsLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDK 209
Cdd:PRK09126  84 NGrspFALTfDARGRGADALGY-LVPNHLIR--RA---------AYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANG 151

                        170       180
                 ....*....|....*....|....*..
gi 675758812 210 ETgdikeLHAPLTVVADGLFSKFRKSL 236
Cdd:PRK09126 152 RR-----LTARLLVAADSRFSATRRQL 173
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 66-232 3.36e-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: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  106 EFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH--DQESKSEVqipYPLSENNQ----VQSGRAFHHGRFIMSLRKAAM 179
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAEllDAEELREL---EPLLPGLRgglfYPDGGHVDPARLLRALARAAE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 675758812  180 AEpNAKFIEGVVLQLLEEDDVVMGVQykdkETGDIKELhapltVVADGLFSKF 232
Cdd:pfam01266 158 AL-GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADL 200
PRK06847 PRK06847
hypothetical protein; Provisional
 67-362 4.74e-06

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 48.72  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTV-------EGLDAQVVNGYMIH 139
Cdd:PRK06847   7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECleagfgfDGVDLFDPDGTLLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 140 DQESKSEVQIPYPlsenNQVQSGR-AFHHgrfImsLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETGdikelH 218
Cdd:PRK06847  87 ELPTPRLAGDDLP----GGGGIMRpALAR---I--LADAARAA-GADVRLGTTVTAIEQDDDGVTVTFSDGTTG-----R 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 219 APLTVVADGLFSKFRKSLVSNK--------------VSVSSHFVGFLMKNAPQFKANhaelilANP-SPVLIYQ--ISSS 281
Cdd:PRK06847 152 YDLVVGADGLYSKVRSLVFPDEpepeytgqgvwravLPRPAEVDRSLMYLGPTTKAG------VVPlSEDLMYLfvTEPR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 282 ETRVLVDvRGEMPRNLREYMVE---KIYPQIPDHLkepfleaTDNSHL--RSMPASFLPPSSVKKRgVLLLGDAYnmrHP 356
Cdd:PRK06847 226 PDNPRIE-PDTLAALLRELLAPfggPVLQELREQI-------TDDAQVvyRPLETLLVPAPWHRGR-VVLIGDAA---HA 293

                        330
                 ....*....|.
gi 675758812 357 LT-----GGGM 362
Cdd:PRK06847 294 TTphlaqGAGM 304
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 67-124 8.27e-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: 8.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHV----------LKDLGLGDT 124
Cdd:COG0569   98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD---PERV--ERLAEEDVLVivgdatdeevLEEAGIEDA 160
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 66-429 1.45e-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: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   66 EVIIVGAGVLGSALAAVLSRD----GRKVTVIERDlKEPDRIVGEFLQPGGY-------------HVLKDLGLGDTVEGL 128
Cdd:TIGR01989   2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDAV-DNPKLKSRNYEKPDGPysnrvssitpasiSFFKKIGAWDHIQSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  129 DAQVVNGYMIHDQESKSEVQipyplsennqvqsgraFHHGRFimslrkaamAEPNAKFIEGVVLQ------LLEEDDVVM 202
Cdd:TIGR01989  81 RIQPFGRMQVWDGCSLALIR----------------FDRDNG---------KEDMACIIENDNIQnslynrLQEYNGDNV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  203 GVQYKDK--------------------ETGDIKELHAPLTVVADGLFSKFRKSlvSNKVSVS-----SHFVGFLMKNAPQ 257
Cdd:TIGR01989 136 KILNPARlisvtipskypndnsnwvhiTLSDGQVLYTKLLIGADGSNSNVRKA--ANIDTTGwnynqHAVVATLKLEEAT 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  258 FKA------------------------------NHAELILANPSPVLIYQISSSetrvLVDVRGEMPR-NLREYMVEKIY 306
Cdd:TIGR01989 214 ENDvawqrflptgpiallplpdnnstlvwstspEEALRLLSLPPEDFVDALNAA----FDLGYSDHPYsYLLDYAMEKLN 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  307 PQIPdHLKE---------PFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIK-LWRKLL 376
Cdd:TIGR01989 290 EDIG-FRTEgskscfqvpPRVIGVVDKSRAAFPLGLGHADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVAsLVKALA 368

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 675758812  377 KGIPDLYDDAAIFEAKKsfYWARKTSHSFVVNILAQALYELFSATDDSLHQLR 429
Cdd:TIGR01989 369 EAVSVGADIGSISSLKP--YERERYAKNVVLLGLVDKLHKLYATDFPPVVALR 419
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
61-101 3.59e-05

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 46.29  E-value: 3.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675758812  61 SQNDPEVIIVGAGVLGSALAAVLSR-DGRKVTVIErdlKEPD 101
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALARELSRyEDLKVLVLE---KEDD 39
trkA PRK09496
Trk system potassium transporter TrkA;
67-135 3.72e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 46.27  E-value: 3.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQpggyhvlkdlglgdtvEGLDAQVVNG 135
Cdd:PRK09496   3 IIIVGAGQVGYTLAENLSGENNDVTVIDTD---EERL--RRLQ----------------DRLDVRTVVG 50
PRK07588 PRK07588
FAD-binding domain;
67-249 5.56e-05

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 45.50  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIER--DLKEPDRIVgEFLQPgGYHVLKDLGLGDTVEGLDAQVVNgymIHDQESK 144
Cdd:PRK07588   3 VAISGAGIAGPTLAYWLRRYGHEPTLIERapELRTGGYMV-DFWGV-GYEVAKRMGITDQLREAGYQIEH---VRSVDPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 145 SEVqipyplSENNQVQSGRAFHHGRFImSLRKAAMAEPNAKFIEGVVLQLL---------EEDDVVMGVQYKDKETGDik 215
Cdd:PRK07588  78 GRR------KADLNVDSFRRMVGDDFT-SLPRGDLAAAIYTAIDGQVETIFddsiatideHRDGVRVTFERGTPRDFD-- 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 675758812 216 elhapLTVVADGLFSKFRkSLVSNKVSVSSHFVG 249
Cdd:PRK07588 149 -----LVIGADGLHSHVR-RLVFGPERDFEHYLG 176
PRK07233 PRK07233
hypothetical protein; Provisional
 69-135 7.27e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 45.26  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  69 IVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVG-----EFlqpGG------YH-----------VLKDLGLGDTV- 125
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEAD----DQLGGlaasfEF---GGlpierfYHhifksdealleLLDELGLEDKLr 76

                         90
                 ....*....|..
gi 675758812 126 --EGLDAQVVNG 135
Cdd:PRK07233  77 wrETKTGYYVDG 88
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 67-131 9.26e-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: 9.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyHVLKDLG----LGDTVEGLDAQ 131
Cdd:COG0446  127 AVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLE----EELREHGvelrLGETVVAIDGD 194
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
69-95 9.30e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.59  E-value: 9.30e-05
                          10        20
                  ....*....|....*....|....*..
gi 675758812   69 IVGAGVLGSALAAVLSRDGRKVTVIER 95
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
PRK06184 PRK06184
hypothetical protein; Provisional
 62-154 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 675758812  62 QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERdLKEP---DRivGEFLQPGGYHVLKDLGLGDTVEGL---------- 128
Cdd:PRK06184   1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEK-APEPfpgSR--GKGIQPRTQEVFDDLGVLDRVVAAgglyppmriy 77

                         90       100
                 ....*....|....*....|....*...
gi 675758812 129 --DAQVVNGYMIHDQESKSEvqIPYPLS 154
Cdd:PRK06184  78 rdDGSVAESDMFAHLEPTPD--EPYPLP 103
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 60-234 1.24e-04

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 44.20  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  60 TSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDL-------KEPD-RIVGefLQPGGYHVLKDLGLGDTVEGL--- 128
Cdd:PRK08020   1 MTNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAApapfdadSQPDvRISA--ISAASVALLKGLGVWDAVQAMrsh 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 129 -----------DAQVVN----------GYMIhdqesksevqipyplsENNQVQsgrafhhgrfiMSLRKAAMAEPNAKFI 187
Cdd:PRK08020  79 pyrrletweweTAHVVFdaaelklpelGYMV----------------ENRVLQ-----------LALWQALEAHPNVTLR 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 675758812 188 EGVVLQLLEEDDVVMGVQYKDKEtgdikELHAPLTVVADGLFSKFRK 234
Cdd:PRK08020 132 CPASLQALQRDDDGWELTLADGE-----EIQAKLVIGADGANSQVRQ 173
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 66-96 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 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERD 96
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 67-109 3.03e-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: 3.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 675758812   67 VIIVGAGVLGSALAAVLSRDGRKVTVIER---DLKEPDRIVGEFLQ 109
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERrdrLLPGFDPEIAKILQ 47
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 67-116 3.23e-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: 40.20  E-value: 3.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 675758812   67 VIIVGAGVLGSALAAVLSRDGrKVTVIERDlkePDRIvgEFLQPGGYHVL 116
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKD---EERV--EELREEGVPVV 44
PRK07538 PRK07538
hypothetical protein; Provisional
 67-236 3.84e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 42.96  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIE--RDLKEPDriVGEFLQPGGYHVLKDLGLGDTvegLDAQVVNGYMI-----H 139
Cdd:PRK07538   3 VLIAGGGIGGLTLALTLHQRGIEVVVFEaaPELRPLG--VGINLLPHAVRELAELGLLDA---LDAIGIRTRELayfnrH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 140 DQESKSE---VQIPYPLSennQVqsgrAFHHGRFIMSLRKAAMAEPNAKFIE---GVVLQLLEEDDVVMGVQykDKETGD 213
Cdd:PRK07538  78 GQRIWSEprgLAAGYDWP---QY----SIHRGELQMLLLDAVRERLGPDAVRtghRVVGFEQDADVTVVFLG--DRAGGD 148

                        170       180
                 ....*....|....*....|...
gi 675758812 214 IKELHAPLTVVADGLFSKFRKSL 236
Cdd:PRK07538 149 LVSVRGDVLIGADGIHSAVRAQL 171
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 67-112 4.08e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 42.19  E-value: 4.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 112
Cdd:PRK08277  14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 67-95 6.35e-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: 6.35e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRD-GRKVTVIER 95
Cdd:COG2303    7 YVIVGAGSAGCVLANRLSEDaGLRVLLLEA 36
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
58-236 6.39e-04

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 42.20  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  58 TSTSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGeflQPGGYH-------VLKDLGLGDTVeGLDA 130
Cdd:PRK06183   4 QHPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW----PTLYD---LPRAVGiddealrVLQAIGLADEV-LPHT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 131 QVVNGYMIHDQESKSEVQIPYPlsennqvqSGRafHHG---RFIMS-------LRKAAMAEPNAKFIEGV-VLQLLEEDD 199
Cdd:PRK06183  76 TPNHGMRFLDAKGRCLAEIARP--------STG--EFGwprRNAFHqplleavLRAGLARFPHVRVRFGHeVTALTQDDD 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 675758812 200 VVMgVQYKDkETGDIKELHAPLTVVADGLFSKFRKSL 236
Cdd:PRK06183 146 GVT-VTLTD-ADGQRETVRARYVVGCDGANSFVRRTL 180
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 67-120 7.28e-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: 41.53  E-value: 7.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 675758812   67 VIIVGAGVLGSALAAVLSRDGRKVTVIE---RDLKEPDRIVGEFLQpggyHVLKDLG 120
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEaldRLLRAFDEEISAALE----KALEKNG 207
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 66-249 8.31e-04

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 41.82  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIV--GEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIhdqeS 143
Cdd:PRK10157   7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVtgGRLYAHSLEHIIPGFADSAPVERLITHEKLAFMT----E 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 144 KSEVQIPYpLSENNQVQSGRAFH--HGRFIMSLRKAAmAEPNAKFIEGV-VLQLLEEDDVVMGVQykdkETGDIKElhAP 220
Cdd:PRK10157  83 KSAMTMDY-CNGDETSPSQRSYSvlRSKFDAWLMEQA-EEAGAQLITGIrVDNLVQRDGKVVGVE----ADGDVIE--AK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 675758812 221 LTVVADGLFSKFRKSL-VSNKVSVSSHFVG 249
Cdd:PRK10157 155 TVILADGVNSILAEKLgMAKRVKPTDVAVG 184
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 67-95 9.09e-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: 9.09e-04
                         10        20
                 ....*....|....*....|....*....
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIER 95
Cdd:COG1233    6 VVVIGAGIGGLAAAALLARAGYRVTVLEK 34
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
67-116 1.03e-03

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 41.25  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYHVL 116
Cdd:COG1226  127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLD---PERV--EELRRFGIKVY 171
PRK00711 PRK00711
D-amino acid dehydrogenase;
66-95 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 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIER 95
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
67-129 1.23e-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: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQpggyHVLKDLG----LGDTVEGLD 129
Cdd:COG1251  145 VVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLlprqldeeAGALLQ----RLLEALGvevrLGTGVTEIE 211
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 67-107 1.57e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.93  E-value: 1.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675758812  67 VIIVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIVGEF 107
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSRLGVKVTVFER----GDRILPLE 208
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 69-125 2.02e-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: 40.23  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 675758812  69 IVGAGVLGSALAAVLSRDGRKVTVIERdlkePDRIvgEFLQPGGYHVLKDLGLGDTV 125
Cdd:COG1893    5 ILGAGAIGGLLGARLARAGHDVTLVAR----GAHA--EALRENGLRLESPDGDRTTV 55
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
61-96 2.35e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 40.55  E-value: 2.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 675758812  61 SQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERD 96
Cdd:COG3573    2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQE 37
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 65-107 2.53e-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: 2.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 675758812  65 PE-VIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGEF 107
Cdd:COG1249  168 PKsLVVIGGGYIGLEFAQIFARLGSEVTLVERG----DRLLPGE 207
PRK07364 PRK07364
FAD-dependent hydroxylase;
58-94 3.47e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 40.00  E-value: 3.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 675758812  58 TSTSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE 94
Cdd:PRK07364  12 PSTRSLTYDVAIVGGGIVGLTLAAALKDSGLRIALIE 48
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
67-234 3.80e-03

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 39.58  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  67 VIIVGAGVLGSALAAVLsRDGR---KVTVIERDLKEP--DRIVGEFLQPGGYHVLKDLGLGDTVEGlDAQVVNGYMIHDQ 141
Cdd:PRK07333   4 VVIAGGGYVGLALAVAL-KQAAphlPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAP-EAQPITDMVITDS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 142 ESKSEVQiPYPLSENNQVQSGRAFHH----GRFIMSLRKAAMAEpNAKFIEGVVLQLLEEDDVVMGVQYKDKETgdikeL 217
Cdd:PRK07333  82 RTSDPVR-PVFLTFEGEVEPGEPFAHmvenRVLINALRKRAEAL-GIDLREATSVTDFETRDEGVTVTLSDGSV-----L 154

                        170
                 ....*....|....*..
gi 675758812 218 HAPLTVVADGLFSKFRK 234
Cdd:PRK07333 155 EARLLVAADGARSKLRE 171
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 66-236 4.49e-03

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 39.37  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKE------PDRIVGEfLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIH 139
Cdd:PRK08850   6 DVAIIGGGMVGLALAAALKESDLRIAVIEGQLPEealnelPDVRVSA-LSRSSEHILRNLGAWQGIEARRAAPYIAMEVW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812 140 DQESksevqipyplsennqvqsgraFHHGRFimslRKAAMAEPN-AKFIEGVVLQL------LEEDDVVM-------GVQ 205
Cdd:PRK08850  85 EQDS---------------------FARIEF----DAESMAQPDlGHIVENRVIQLalleqvQKQDNVTLlmparcqSIA 139

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 675758812 206 YKDKET----GDIKELHAPLTVVADGLFSKFRKSL 236
Cdd:PRK08850 140 VGESEAwltlDNGQALTAKLVVGADGANSWLRRQM 174
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
65-95 4.51e-03

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 39.09  E-value: 4.51e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 675758812  65 PEVIIVGAGVLGSALAAVLSRDGRKVTVIER 95
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEK 34
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 63-96 4.59e-03

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 39.21  E-value: 4.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERD 96
Cdd:PRK07688  23 REKHVLIIGAGALGTANAEMLVRAGvGKVTIVDRD 57
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 67-104 5.54e-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: 5.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 675758812   67 VIIVGAGVLGSALAAVLSRDG--RKVTVIERDLKEPDRIV 104
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALA 40
PRK06370 PRK06370
FAD-containing oxidoreductase;
68-97 5.80e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 39.03  E-value: 5.80e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 675758812  68 IIVGAGVLGSALAAVLSRDGRKVTVIERDL 97
Cdd:PRK06370   9 IVIGAGQAGPPLAARAAGLGMKVALIERGL 38
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
55-129 6.44e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 38.74  E-value: 6.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675758812  55 AACTSTSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLG----LGDTVEGLD 129
Cdd:PRK04965 132 RAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGvhllLKSQLQGLE 210
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 65-123 6.57e-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: 6.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675758812  65 PEVIIVGAGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQPGGYHV-----------LKDLGLGD 123
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS----DRVgglirtveVDGFRIDRGPHSfltrdpevlelLRELGLGD 75
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
66-130 7.03e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 38.73  E-value: 7.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675758812  66 EVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPgGYHVLKDLGLGDTVEGLDA 130
Cdd:PRK07494   9 DIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGP-SIRFLERLGLWARLAPHAA 72
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 66-204 7.25e-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: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675758812   66 EVIIVGAGVLGSALAAVLSRD-GRKVTVIERDLkepdrivgeflQPGGyhvlkdlGLGdtvegLDAQVVNgYMIHDQESK 144
Cdd:pfam01946  19 DVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSV-----------SPGG-------GAW-----LGGQLFS-AMVVRKPAH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675758812  145 ---SEVQIPYPLSENNQVQSgrafHHGRFIMSLRKAAMAEPNAKFIEGVVLQ--LLEEDDVVMGV 204
Cdd:pfam01946  75 lflDEFGIPYEDEGDYVVVK----HAALFTSTLMSKALQLPNVKLFNATSVEdlIVRPGVGVAGV 135
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
59-96 7.86e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 38.75  E-value: 7.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675758812  59 STSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIE-RD 96
Cdd:COG1231    2 SRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD 40
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 64-99 8.19e-03

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 38.56  E-value: 8.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 675758812  64 DPEVIIVGAGVLGSALAAVLSRDG-RKVTVIERDLKE 99
Cdd:PRK12475  24 EKHVLIVGAGALGAANAEALVRAGiGKLTIADRDYVE 60
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 63-112 8.26e-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: 8.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 675758812  63 NDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 112
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGG 54
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 59-95 8.98e-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: 38.69  E-value: 8.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 675758812  59 STSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIER 95
Cdd:COG2072    1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
 
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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