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Conserved domains on  [gi|1952977115|ref|XP_038411426|]
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squalene monooxygenase [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 276-547 7.45e-148

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member pfam08491:

Pssm-ID: 473865  Cd Length: 276  Bit Score: 426.75  E-value: 7.45e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 276 HAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLVDIRGE-MPR- 353
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 354 ---NLREYMAEKIYPQLPDHLKEPFLEAIQNSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTGGGMTVVFKDLKLW 430
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 431 RKLLKSIPDLYDDAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAKDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 510
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1952977115 511 LSPNPLILIGHFFAVALYATYFCFKSEPWITKPRAIF 547
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
134-421 2.25e-16

Dehydrogenase (flavoprotein) [Energy production and conversion];


:

Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 79.63  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 134 GSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEdidaQVVDGYIIHDQDSKSeVQIPYPVSE 213
Cdd:COG0644     5 GSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSPGGKS-VELPPGRGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 214 NSQVRsgRAfhhgRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMgVqyrdkETGDVKELHAPLTVVADGLFSKFRK 292
Cdd:COG0644    80 GYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARSLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 293 NLISNKVSVSSHFVGFLMK------NAPQFKANHAELILTNPSPV-LIYQISSNETRVLVDIrgemprnlreymaekiyp 365
Cdd:COG0644   147 KLGLKRRSDEPQDYALAIKehwelpPLEGVDPGAVEFFFGEGAPGgYGWVFPLGDGRVSVGI------------------ 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952977115 366 qlpdhlkepfleaiqnsrlrsmPASFLPSSPVnKRGVLLLGDAYNMRHPLTGGGMT 421
Cdd:COG0644   209 ----------------------PLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIH 241
 
Name Accession Description Interval E-value
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 276-547 7.45e-148

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: 426.75  E-value: 7.45e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 276 HAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLVDIRGE-MPR- 353
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 354 ---NLREYMAEKIYPQLPDHLKEPFLEAIQNSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTGGGMTVVFKDLKLW 430
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 431 RKLLKSIPDLYDDAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAKDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 510
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1952977115 511 LSPNPLILIGHFFAVALYATYFCFKSEPWITKPRAIF 547
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 122-567 8.20e-126

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 381.12  E-value: 8.20e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVvDGYIIHDQD 200
Cdd:PTZ00367   33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 201 SKsEVQIPYpvsenSQVRSGRAFHHGRFIMGLRKAAMA--EPNTKFIEGIVLQLLEED----DAVMGVQYRDKETGDV-- 272
Cdd:PTZ00367  112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDVpe 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 273 ------------------KELHAPLTVVADGLFSKFRKNLISNKVSVS--SHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PTZ00367  186 npfredppsanpsattvrKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 333 IYQISSNETRVLVDIRGEMPRNLRE---YMAEKIYPQLPDHLKEPFLEAIQN-SRLRSMPASFLPSSPVNKRGVLLLGDA 408
Cdd:PTZ00367  266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASKDtKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 409 YNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYD---------DAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAK 479
Cdd:PTZ00367  346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 480 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVALYA--------------------TYFCFKSEPW 539
Cdd:PTZ00367  425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGvlnlimetgaysifgkqlssFEKLTNVASF 499

                         490       500
                  ....*....|....*....|....*...
gi 1952977115 540 ITKPRAIFSSGAVLYKACSVIFPLIYSE 567
Cdd:PTZ00367  500 FVDPERIKHALYLLGAATTIAAPLAKSE 527
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 120-489 3.14e-21

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: 95.00  E-value: 3.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIdAQVVDGYIIHDQ 199
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 DSKSEV-QIPYPVsenSQVRSGRAFHHGRFIMGLRKAAmAEPNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeLHAP 278
Cdd:COG0654    80 SDGRVLaRFDAAE---TGLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 279 LTVVADGLFSKFRKnlisnkvsvsSHFVGFLMKNAPQfkanhaeliltnpspvliyqissneTRVLVDIRGEMprnlrey 358
Cdd:COG0654   151 LVVGADGARSAVRR----------LLGIGFTGRDYPQ-------------------------RALWAGVRTEL------- 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 359 maEKIYPQLPDHLKEpFLEAIQNSRLrsmPASFLPSSPVNKRGVLLLGDA-YNMrHPLTGGGMTVVFKD-LKLWRKLLKS 436
Cdd:COG0654   189 --RARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDaAALAWKLAAA 261

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952977115 437 IPDLyDDAAVFQAkksfYW-ERKTSHSFVVNiLAQALYELFSAKDDSLHQLRKA 489
Cdd:COG0654   262 LRGR-DDEAALAR----YErERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
134-421 2.25e-16

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 79.63  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 134 GSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEdidaQVVDGYIIHDQDSKSeVQIPYPVSE 213
Cdd:COG0644     5 GSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSPGGKS-VELPPGRGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 214 NSQVRsgRAfhhgRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMgVqyrdkETGDVKELHAPLTVVADGLFSKFRK 292
Cdd:COG0644    80 GYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARSLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 293 NLISNKVSVSSHFVGFLMK------NAPQFKANHAELILTNPSPV-LIYQISSNETRVLVDIrgemprnlreymaekiyp 365
Cdd:COG0644   147 KLGLKRRSDEPQDYALAIKehwelpPLEGVDPGAVEFFFGEGAPGgYGWVFPLGDGRVSVGI------------------ 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952977115 366 qlpdhlkepfleaiqnsrlrsmPASFLPSSPVnKRGVLLLGDAYNMRHPLTGGGMT 421
Cdd:COG0644   209 ----------------------PLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIH 241
PRK07045 PRK07045
putative monooxygenase; Reviewed
 121-426 9.13e-16

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 79.18  E-value: 9.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVVDGY-IIHDQ 199
Cdd:PRK07045    4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 DSKSevqipypvSENSQVRSGRAFhhgrFIM----GLRKAAMA----EPNTKFIEGIVLQLLE--EDDAVMGVQYRDKET 269
Cdd:PRK07045   84 ELIA--------SLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGER 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 270 gdvkelHAPLTVV-ADGLFSKFRKNLI---SNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLV 345
Cdd:PRK07045  152 ------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLVV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 346 DIRGEmprNLREYMA----EKIYPQLPDHLKEPFLEAIQ----NSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTG 417
Cdd:PRK07045  226 SFPAD---EMQGYLAdttrTKLLARLNEFVGDESADAMAaigaGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITG 302


                  ....*....
gi 1952977115 418 GGMTVVFKD 426
Cdd:PRK07045  303 QGMNLAIED 311
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 124-369 4.43e-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: 48.93  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 163
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 164 EFLQPGGYRVLEDLGLKDAVEDIDAQVVDGYIIHDQDSKSEVQIpYPVSENSQ----VRSGRAFHHGRFIMGLRKAAMAE 239
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAELLDAEELREL-EPLLPGLRgglfYPDGGHVDPARLLRALARAAEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 240 pNTKFIEGIVLQLLEEDDAVMGVQyrdkETGDVKELhapltVVADGLFSKF-RKNLISNKVSVSSHFVGFLMKnaPQFKA 318
Cdd:pfam01266 160 -GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADLlALPGLRLPVRPVRGQVLVLEP--LPEAL 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952977115 319 NHAELILTNPSPVLIYQISSNETRVLV--------DIRGEMPRNLREYM---AEKIYPQLPD 369
Cdd:pfam01266 228 LILPVPITVDPGRGVYLRPRADGRLLLggtdeedgFDDPTPDPEEIEELleaARRLFPALAD 289
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 121-189 1.77e-04

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: 43.60  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952977115 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG------YRVLEDLGLKDAVEDIDAQ 189
Cdd:cd08935     5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGraialaADVLDRASLERAREEIVAQ 79
 
Name Accession Description Interval E-value
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 276-547 7.45e-148

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: 426.75  E-value: 7.45e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 276 HAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLVDIRGE-MPR- 353
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPkLPSi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 354 ---NLREYMAEKIYPQLPDHLKEPFLEAIQNSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTGGGMTVVFKDLKLW 430
Cdd:pfam08491  81 angELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 431 RKLLKSIPDLYDDAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAKDDSLHQLRKACFLYFKLGGECVAGPVGLLSV 510
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKP-YDAVINTLSIALYSLFAADSDELKALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1952977115 511 LSPNPLILIGHFFAVALYATYFCFKSEPWITKPRAIF 547
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGSPLALL 276
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 122-567 8.20e-126

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 381.12  E-value: 8.20e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLK-EPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVvDGYIIHDQD 200
Cdd:PTZ00367   33 DYDVIIVGGSIAGPVLAKALSKQGRKVLMLERDLFsKPDRIVGELLQPGGVNALKELGMEECAEGIGMPC-FGYVVFDHK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 201 SKsEVQIPYpvsenSQVRSGRAFHHGRFIMGLRKAAMA--EPNTKFIEGIVLQLLEED----DAVMGVQYRDKETGDV-- 272
Cdd:PTZ00367  112 GK-QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHncQDNVTMLEGTVNSLLEEGpgfsERAYGVEYTEAEKYDVpe 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 273 ------------------KELHAPLTVVADGLFSKFRKNLISNKVSVS--SHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PTZ00367  186 npfredppsanpsattvrKVATAPLVVMCDGGMSKFKSRYQHYTPASEnhSHFVGLVLKNVRLPKEQHGTVFLGKTGPIL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 333 IYQISSNETRVLVDIRGEMPRNLRE---YMAEKIYPQLPDHLKEPFLEAIQN-SRLRSMPASFLPSSPVNKRGVLLLGDA 408
Cdd:PTZ00367  266 SYRLDDNELRVLVDYNKPTLPSLEEqseWLIEDVAPHLPENMRESFIRASKDtKRIRSMPNARYPPAFPSIKGYVGIGDH 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 409 YNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYD---------DAAVFQAKKSFYWERKTsHSFVVNILAQALYELFSAK 479
Cdd:PTZ00367  346 ANQRHPLTGGGMTCCFSDCIRLAKSLTGIKSLRSidqnemaeiEDAIQAAILSYARNRKT-HASTINILSWALYSVFSSP 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 480 ddslhQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVALYA--------------------TYFCFKSEPW 539
Cdd:PTZ00367  425 -----ALRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGvlnlimetgaysifgkqlssFEKLTNVASF 499

                         490       500
                  ....*....|....*....|....*...
gi 1952977115 540 ITKPRAIFSSGAVLYKACSVIFPLIYSE 567
Cdd:PTZ00367  500 FVDPERIKHALYLLGAATTIAAPLAKSE 527
PLN02985 PLN02985
squalene monooxygenase
 95-527 3.67e-101

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 315.69  E-value: 3.67e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115  95 SRRHKKGTSISEttligaAASSIPSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVL 174
Cdd:PLN02985   22 TNRKKKATELAD------AVAEERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERMMGEFMQPGGRFML 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 175 EDLGLKDAVEDIDAQVVDGYIIHdQDSKsEVQIPYPVSEN--SQVRSGRAFHHGRFIMGLRKAAMAEPNTKFIEGIVLQL 252
Cdd:PLN02985   96 SKLGLEDCLEGIDAQKATGMAVY-KDGK-EAVAPFPVDNNnfPYEPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 253 LEEDDAVMGVQYRDKETGDVKELhAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVL 332
Cdd:PLN02985  174 IEEKGVIKGVTYKNSAGEETTAL-APLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEEPEKLHLIMSKPSFTM 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 333 IYQISSNETRVLVDI---------RGEMPRNLREYMAekiyPQLPDHLKEPFLEAI-QNSRLRSMPASFLPSSPVNKRGV 402
Cdd:PLN02985  253 LYQISSTDVRCVFEVlpdnipsiaNGEMSTFVKNTIA----PQVPPKLRKIFLKGIdEGAHIKVVPTKRMSATLSDKKGV 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 403 LLLGDAYNMRHPLTGGGMTVVFKDLKLWRKLLKSIPDLYDDAAVFQAKKSFYWERKtSHSFVVNILAQALYE-LFSAKDD 481
Cdd:PLN02985  329 IVLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRK-PMSATVNTLGNAFSQvLVASTDE 407

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1952977115 482 SLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLILIGHFFAVAL 527
Cdd:PLN02985  408 AKEAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITL 453
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 120-489 3.14e-21

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: 95.00  E-value: 3.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIdAQVVDGYIIHDQ 199
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLAR-GAPIRGIRVRDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 DSKSEV-QIPYPVsenSQVRSGRAFHHGRFIMGLRKAAmAEPNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeLHAP 278
Cdd:COG0654    80 SDGRVLaRFDAAE---TGLPAGLVVPRADLERALLEAA-RALGVELRFGTEVTGLEQDADGVTVTLADGRT-----LRAD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 279 LTVVADGLFSKFRKnlisnkvsvsSHFVGFLMKNAPQfkanhaeliltnpspvliyqissneTRVLVDIRGEMprnlrey 358
Cdd:COG0654   151 LVVGADGARSAVRR----------LLGIGFTGRDYPQ-------------------------RALWAGVRTEL------- 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 359 maEKIYPQLPDHLKEpFLEAIQNSRLrsmPASFLPSSPVNKRGVLLLGDA-YNMrHPLTGGGMTVVFKD-LKLWRKLLKS 436
Cdd:COG0654   189 --RARLAAAGPRLGE-LLELSPRSAF---PLRRRRAERWRRGRVVLLGDAaHTM-HPLGGQGANLALRDaAALAWKLAAA 261

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952977115 437 IPDLyDDAAVFQAkksfYW-ERKTSHSFVVNiLAQALYELFSAKDDSLHQLRKA 489
Cdd:COG0654   262 LRGR-DDEAALAR----YErERRPRAARVQR-AADALGRLFHPDSPPLRLLRNA 309
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
134-421 2.25e-16

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 79.63  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 134 GSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEdidaQVVDGYIIHDQDSKSeVQIPYPVSE 213
Cdd:COG0644     5 GSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLE----RPVRGARFYSPGGKS-VELPPGRGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 214 NSQVRsgRAfhhgRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMgVqyrdkETGDVKELHAPLTVVADGLFSKFRK 292
Cdd:COG0644    80 GYVVD--RA----RFDRWLAEQA-EEAGAEVRTGTrVTDVLRDDGRVV-V-----RTGDGEEIRADYVVDADGARSLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 293 NLISNKVSVSSHFVGFLMK------NAPQFKANHAELILTNPSPV-LIYQISSNETRVLVDIrgemprnlreymaekiyp 365
Cdd:COG0644   147 KLGLKRRSDEPQDYALAIKehwelpPLEGVDPGAVEFFFGEGAPGgYGWVFPLGDGRVSVGI------------------ 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952977115 366 qlpdhlkepfleaiqnsrlrsmPASFLPSSPVnKRGVLLLGDAYNMRHPLTGGGMT 421
Cdd:COG0644   209 ----------------------PLGGPRPRLV-GDGVLLVGDAAGFVDPLTGEGIH 241
PRK07045 PRK07045
putative monooxygenase; Reviewed
 121-426 9.13e-16

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 79.18  E-value: 9.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDIDAQVVDGY-IIHDQ 199
Cdd:PRK07045    4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMrLYHDK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 DSKSevqipypvSENSQVRSGRAFhhgrFIM----GLRKAAMA----EPNTKFIEGIVLQLLE--EDDAVMGVQYRDKET 269
Cdd:PRK07045   84 ELIA--------SLDYRSASALGY----FILipceQLRRLLLAkldgLPNVRLRFETSIERIErdADGTVTSVTLSDGER 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 270 gdvkelHAPLTVV-ADGLFSKFRKNLI---SNKVSVSSHFVGFLMKNAPQFKANHAELILTNPSPVLIYQISSNETRVLV 345
Cdd:PRK07045  152 ------VAPTVLVgADGARSMIRDDVLrmpAERVPYATPMAFGTIALTDSVRECNRLYVDSNQGLAYFYPIGDQATRLVV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 346 DIRGEmprNLREYMA----EKIYPQLPDHLKEPFLEAIQ----NSRLRSMPASFLPSSPVNKRGVLLLGDAYNMRHPLTG 417
Cdd:PRK07045  226 SFPAD---EMQGYLAdttrTKLLARLNEFVGDESADAMAaigaGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITG 302


                  ....*....
gi 1952977115 418 GGMTVVFKD 426
Cdd:PRK07045  303 QGMNLAIED 311
PRK06185 PRK06185
FAD-dependent oxidoreductase;
124-292 3.53e-14

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 74.51  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIE------RDLKepdrivGEFLQPGGYRVLEDLGLKDAVEDIDaqvvdgyiiH 197
Cdd:PRK06185    8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDFR------GDTVHPSTLELMDELGLLERFLELP---------H 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 198 DQDSKSEVQIPypvseNSQVRS---GRAFHHGRFIM---------GLRKAAMAEPNTKFIEG-IVLQLLEEDDAVMGVQY 264
Cdd:PRK06185   73 QKVRTLRFEIG-----GRTVTLadfSRLPTPYPYIAmmpqwdfldFLAEEASAYPNFTLRMGaEVTGLIEEGGRVTGVRA 147

                         170       180
                  ....*....|....*....|....*...
gi 1952977115 265 RDKEtGDVkELHAPLTVVADGLFSKFRK 292
Cdd:PRK06185  148 RTPD-GPG-EIRADLVVGADGRHSRVRA 173
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
119-306 1.53e-11

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 66.21  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 119 SQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIErdlkEPDRIvGEF-----LQPGGYRVLEDLGLKDAVEDIdAQVVDG 193
Cdd:PRK08163    1 MTKVTPVLIVGGGIGGLAAALALARQGIKVKLLE----QAAEI-GEIgagiqLGPNAFSALDALGVGEAARQR-AVFTDH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 194 YIIHD-QDSKSEVQIpyPVSENSQVRSG-------RAFHHGRFImglrKAAMAEPNTKFIEGIVLQLLEEDDAvmGVQYR 265
Cdd:PRK08163   75 LTMMDaVDAEEVVRI--PTGQAFRARFGnpyavihRADIHLSLL----EAVLDHPLVEFRTSTHVVGIEQDGD--GVTVF 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952977115 266 DKETgdvKELHAPLTVVADGLFSKFRKNLISNKVSVSSHFV 306
Cdd:PRK08163  147 DQQG---NRWTGDALIGCDGVKSVVRQSLVGDAPRVTGHVV 184
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 122-420 1.05e-10

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: 63.50  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 122 DPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIV---GEFLQPGGYRVLEDLGLKDAVEDIDA---------Q 189
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERH---ATTSVlprAHGLNQRTMELLRQAGLEDRILAEGVphegmglafY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 190 VVDGYIIHDQDSKSEVQIPYPVSENSQVrsgrafhhgrfimgLRKAAMAEPnTKFIEGIVLQLLEEDDAVMGVQYRDKET 269
Cdd:pfam01494  78 NTRRRADLDFLTSPPRVTVYPQTELEPI--------------LVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRDRRD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 270 GDVKELHAPLTVVADGLFSKFRKNL---ISNKVSVSSHFVG--FLMKNAPQFKANHA--ELILTNPSPVLIYQISSNETR 342
Cdd:pfam01494 143 GEEYTVRAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDvlFDAPDLSDPVERAFvhYLIYAPHSRGFMVGPWRSAGR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 343 VLVDIRGEmprnLREYMAEKIYPQLPDHLKEPFLEAIQNSRLrsmPASFLPSS--PVNKR--------GVLLLGDAYNmR 412
Cdd:pfam01494 223 ERYYVQVP----WDEEVEERPEEFTDEELKQRLRSIVGIDLA---LVEILWKSiwGVASRvatryrkgRVFLAGDAAH-I 294


                  ....*....
gi 1952977115 413 HPLTGG-GM 420
Cdd:pfam01494 295 HPPTGGqGL 303
PRK06847 PRK06847
hypothetical protein; Provisional
 125-292 4.55e-08

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 55.26  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYRVLEDLGLKDAVEDiDAQVVDGYIIHDQDSKSE 204
Cdd:PRK06847    7 VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECLE-AGFGFDGVDLFDPDGTLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 205 VQIPYPVSENSQVRSG-----RAFHHgrfImgLRKAAMAEpNTKFIEGIVLQLLEEDDAVMGVQYRDKETGdvkelHAPL 279
Cdd:PRK06847   86 AELPTPRLAGDDLPGGggimrPALAR---I--LADAARAA-GADVRLGTTVTAIEQDDDGVTVTFSDGTTG-----RYDL 154

                         170
                  ....*....|...
gi 1952977115 280 TVVADGLFSKFRK 292
Cdd:PRK06847  155 VVGADGLYSKVRS 167
PRK09126 PRK09126
FAD-dependent hydroxylase;
125-294 1.49e-07

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 53.79  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD----LKEPD---RIVGefLQPGGYRVLEDLGLKDAVEDI------DAQVV 191
Cdd:PRK09126    6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQplaaLADPAfdgREIA--LTHASREILQRLGAWDRIPEDeisplrDAKVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 192 DG---YIIH-DQDSKSEVQIPYPVSeNSQVRsgRAfhhgrfimgLRKAAMAEPNTKFIEGIVLQLLEEDDAVMGVQYRDK 267
Cdd:PRK09126   84 NGrspFALTfDARGRGADALGYLVP-NHLIR--RA---------AYEAVSQQDGIELLTGTRVTAVRTDDDGAQVTLANG 151

                         170       180
                  ....*....|....*....|....*..
gi 1952977115 268 ETgdvkeLHAPLTVVADGLFSKFRKNL 294
Cdd:PRK09126  152 RR-----LTARLLVAADSRFSATRRQL 173
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 124-369 4.43e-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: 48.93  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD----------------------------------------LKEPDRIVG 163
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGddpgsgasgrnaglihpglrylepselarlalealdlweeLEEELGIDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 164 EFLQPGGYRVLEDLGLKDAVEDIDAQVVDGYIIHDQDSKSEVQIpYPVSENSQ----VRSGRAFHHGRFIMGLRKAAMAE 239
Cdd:pfam01266  81 GFRRCGVLVLARDEEEEALEKLLAALRRLGVPAELLDAEELREL-EPLLPGLRgglfYPDGGHVDPARLLRALARAAEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 240 pNTKFIEGIVLQLLEEDDAVMGVQyrdkETGDVKELhapltVVADGLFSKF-RKNLISNKVSVSSHFVGFLMKnaPQFKA 318
Cdd:pfam01266 160 -GVRIIEGTEVTGIEEEGGVWGVV----TTGEADAV-----VNAAGAWADLlALPGLRLPVRPVRGQVLVLEP--LPEAL 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952977115 319 NHAELILTNPSPVLIYQISSNETRVLV--------DIRGEMPRNLREYM---AEKIYPQLPD 369
Cdd:pfam01266 228 LILPVPITVDPGRGVYLRPRADGRLLLggtdeedgFDDPTPDPEEIEELleaARRLFPALAD 289
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
125-154 1.06e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 47.98  E-value: 1.06e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD 154
Cdd:COG0665     5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 125-182 1.64e-05

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: 46.98  E-value: 1.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYRV----------LEDLGLKDA 182
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD---PERV--ERLAEEDVLVivgdatdeevLEEAGIEDA 160
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 124-411 3.04e-05

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 46.44  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIV--GEFLQPGGYRVLEDLGLKDAVEDIdaqvvdgyIIHDQ-- 199
Cdd:PRK10157    7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVtgGRLYAHSLEHIIPGFADSAPVERL--------ITHEKla 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 --DSKSEVQIPYpVSENSQVRSGRAFH--HGRFIMGLRKAAmAEPNTKFIEGI-VLQLLEEDDAVMGVQyrdkETGDVKE 274
Cdd:PRK10157   79 fmTEKSAMTMDY-CNGDETSPSQRSYSvlRSKFDAWLMEQA-EEAGAQLITGIrVDNLVQRDGKVVGVE----ADGDVIE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 275 lhAPLTVVADGLFSKFRKNL-ISNKVSVSSHFVGF---------LMKNAPQFKANHAELILTNPSPV-------LIYqis 337
Cdd:PRK10157  153 --AKTVILADGVNSILAEKLgMAKRVKPTDVAVGVkelielpksVIEDRFQLQGNQGAACLFAGSPTdglmgggFLY--- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 338 SNETRVLVDIRGEMpRNLREymAEKIYPQLPDHLKEPFLEA--IQNSRLRSMPASFLPSSPVNKR------GVLLLGDAY 409
Cdd:PRK10157  228 TNENTLSLGLVCGL-HHLHD--AKKSVPQMLEDFKQHPAVAplIAGGKLVEYSAHVVPEAGINMLpelvgdGVLIAGDAA 304


                  ..
gi 1952977115 410 NM 411
Cdd:PRK10157  305 GM 306
PRK06184 PRK06184
hypothetical protein; Provisional
 120-294 6.03e-05

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 45.75  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 120 QNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERdLKEP---DRivGEFLQPGGYRVLEDLGLKDAV-----------ED 185
Cdd:PRK06184    1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEK-APEPfpgSR--GKGIQPRTQEVFDDLGVLDRVvaagglyppmrIY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 186 IDAQVVDGYIIHDqDSKSEVQIPYPvseNS----QVRSGRafhhgrfIMGLRKAAMA---EPNTKFIEgivlqlLEEDDA 258
Cdd:PRK06184   78 RDDGSVAESDMFA-HLEPTPDEPYP---LPlmvpQWRTER-------ILRERLAELGhrvEFGCELVG------FEQDAD 140

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952977115 259 vmGVQYRDKETGDVKELHAPLTVVADGLFSKFRKNL 294
Cdd:PRK06184  141 --GVTARVAGPAGEETVRARYLVGADGGRSFVRKAL 174
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
124-292 6.28e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 45.66  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPgGYRVLEDLGLKDAVEDIDA-----QVVDgyiihd 198
Cdd:PRK07494    9 DIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGP-SIRFLERLGLWARLAPHAAplqsmRIVD------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 199 qDSKSEVQIPyPVSENSQVRSGRAFhhG------RFIMGLRKAAMAEPN-TKFiegivlqlleeDDAVMGVQYRDKE--- 268
Cdd:PRK07494   82 -ATGRLIRAP-EVRFRAAEIGEDAF--GynipnwLLNRALEARVAELPNiTRF-----------GDEAESVRPREDEvtv 146

                         170       180
                  ....*....|....*....|....*
gi 1952977115 269 -TGDVKELHAPLTVVADGLFSKFRK 292
Cdd:PRK07494  147 tLADGTTLSARLVVGADGRNSPVRE 171
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
118-285 7.11e-05

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 45.67  E-value: 7.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 118 PSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRIVGeflQPGG-------YRVLEDLGLkdaVEDIDAQV 190
Cdd:PRK06183    6 PDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW----PTLYD---LPRAvgiddeaLRVLQAIGL---ADEVLPHT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 191 VDGYIIHDQDSKSEV--QIPYPvsensqvrSGRafHHG-----RFIM-----GLRKAAMAEPNTKFIEGI-VLQLLEEDD 257
Cdd:PRK06183   76 TPNHGMRFLDAKGRClaEIARP--------STG--EFGwprrnAFHQplleaVLRAGLARFPHVRVRFGHeVTALTQDDD 145

                         170       180
                  ....*....|....*....|....*...
gi 1952977115 258 AVMgVQYRDkETGDVKELHAPLTVVADG 285
Cdd:PRK06183  146 GVT-VTLTD-ADGQRETVRARYVVGCDG 171
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 125-180 7.50e-05

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: 41.42  E-value: 7.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIER---DLKEPDRIVGEFLQpggyRVLEDLGLK 180
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERrdrLLPGFDPEIAKILQ----EKLEKNGIE 56
PRK07538 PRK07538
hypothetical protein; Provisional
 125-186 8.81e-05

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 45.27  E-value: 8.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIE--RDLKEPDriVGEFLQPGGYRVLEDLGLKDAVEDI 186
Cdd:PRK07538    3 VLIAGGGIGGLTLALTLHQRGIEVVVFEaaPELRPLG--VGINLLPHAVRELAELGLLDALDAI 64
trkA PRK09496
Trk system potassium transporter TrkA;
125-182 1.12e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 44.73  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDR------------IVGEFLQPggyRVLEDLGLKDA 182
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTD---EERlrrlqdrldvrtVVGNGSSP---DVLREAGAEDA 66
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
127-153 1.72e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 39.82  E-value: 1.72e-04
                          10        20
                  ....*....|....*....|....*..
gi 1952977115 127 IVGSGVLGSALAAVLSRDGRKVTVIER 153
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 125-170 1.74e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 43.74  E-value: 1.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG 170
Cdd:PRK08277   14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 121-189 1.77e-04

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: 43.60  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952977115 121 NDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGG------YRVLEDLGLKDAVEDIDAQ 189
Cdd:cd08935     5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGraialaADVLDRASLERAREEIVAQ 79
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 123-209 2.08e-04

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: 43.92  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 123 PE-VIIVGSGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyRVLEDLGLK-------DAVEDIDaqvv 191
Cdd:COG1249   168 PKsLVVIGGGYIGLEFAQIFARLGSEVTLVERGdrlLPGEDPEISEALE----KALEKEGIDiltgakvTSVEKTG---- 239

                          90
                  ....*....|....*...
gi 1952977115 192 DGYIIHDQDSKSEVQIPY 209
Cdd:COG1249   240 DGVTVTLEDGGGEEAVEA 257
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
119-159 3.11e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 43.21  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1952977115 119 SQNDPEVIIVGSGVLGSALAAVLSR-DGRKVTVIErdlKEPD 159
Cdd:COG0579     1 MMEMYDVVIIGAGIVGLALARELSRyEDLKVLVLE---KEDD 39
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 125-180 6.49e-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: 6.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIE---RDLKEPDRIVGEFLQpggyRVLEDLGLK 180
Cdd:pfam07992 155 VVVVGGGYIGVELAAALAKLGKEVTLIEaldRLLRAFDEEISAALE----KALEKNGVE 209
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 125-184 8.20e-04

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.14  E-value: 8.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRI---VGEFLQPG---------------GYRVLEDLGLKDAVE 184
Cdd:COG1233     6 VVVIGAGIGGLAAAALLARAGYRVTVLEKN----DTPggrARTFERPGfrfdvgpsvltmpgvLERLFRELGLEDYLE 79
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 125-189 8.47e-04

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: 41.72  E-value: 8.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERD---LKEPDRIVGEFLQpggyRVLEDLG----LKDAVEDIDAQ 189
Cdd:COG0446   127 AVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLE----EELREHGvelrLGETVVAIDGD 194
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
112-182 9.07e-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: 9.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 112 AAASSIPSQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDlkePDRIvgEFLQPGGYRV----------LEDLGLKD 181
Cdd:COG1226   114 AEAAEDAIDLEGHVIIAGFGRVGQIVARLLRAEGIPFVVIDLD---PERV--EELRRFGIKVyygdatrpdvLEAAGIER 188


                  .
gi 1952977115 182 A 182
Cdd:COG1226   189 A 189
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 119-292 9.51e-04

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 41.89  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 119 SQNDPEVIIVGSGVLGSALAAVLSRDGRKVTVIERDL-------KEPD-RIVGefLQPGGYRVLEDLGLKDAVEDI---- 186
Cdd:PRK08020    2 TNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEHAApapfdadSQPDvRISA--ISAASVALLKGLGVWDAVQAMrshp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 187 ----------DAQVVdgyiiHDQDSKSEVQIPYPVsENSQVRsgrafhhgrfiMGLRKAAMAEPNTKFIEGIVLQLLEED 256
Cdd:PRK08020   80 yrrletweweTAHVV-----FDAAELKLPELGYMV-ENRVLQ-----------LALWQALEAHPNVTLRCPASLQALQRD 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1952977115 257 DAVMGVQYRDKEtgdvkELHAPLTVVADGLFSKFRK 292
Cdd:PRK08020  143 DDGWELTLADGE-----EIQAKLVIGADGANSQVRQ 173
PRK00711 PRK00711
D-amino acid dehydrogenase;
124-153 1.01e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 41.71  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIER 153
Cdd:PRK00711    2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 125-153 1.50e-03

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: 41.35  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRD-GRKVTVIER 153
Cdd:COG2303     7 YVIVGAGSAGCVLANRLSEDaGLRVLLLEA 36
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 124-154 1.96e-03

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: 40.99  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1952977115 124 EVIIVGSGVLGSALAAVLSRDGRKVTVIERD 154
Cdd:PRK01747  262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
125-187 2.21e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 40.51  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRI--------VGEFLQpggyRVLEDLG----LKDAVEDID 187
Cdd:COG1251   145 VVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLlprqldeeAGALLQ----RLLEALGvevrLGTGVTEIE 211
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 123-165 2.30e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.55  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1952977115 123 PE-VIIVGSGVLGSALAAVLSRDGRKVTVIERdlkePDRIVGEF 165
Cdd:PRK06292  169 PKsLAVIGGGVIGLELGQALSRLGVKVTVFER----GDRILPLE 208
PRK07233 PRK07233
hypothetical protein; Provisional
 125-184 2.49e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 40.64  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDlkepDRIVG-----EFlqpGGYRV-----------------LEDLGLKDA 182
Cdd:PRK07233    2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEAD----DQLGGlaasfEF---GGLPIerfyhhifksdeallelLDELGLEDK 74


                  ..
gi 1952977115 183 VE 184
Cdd:PRK07233   75 LR 76
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 125-191 3.40e-03

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


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 39.61  E-value: 3.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952977115 125 VIIVGSGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPggyrVLEDLGLKDAVEDIDAQVV 191
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTP----LAADLTQPGLLADVDHLVI 63
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 127-178 5.79e-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: 39.07  E-value: 5.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952977115 127 IVGSGVLGSALAAVLSRDGRKVTVIERdlkePDRIvgEFLQPGGYRVLEDLG 178
Cdd:COG1893     5 ILGAGAIGGLLGARLARAGHDVTLVAR----GAHA--EALRENGLRLESPDG 50
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
125-292 7.32e-03

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 38.81  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 125 VIIVGSGVLGSALAAVLsRDGR---KVTVIERDLKEP--DRIVGEFLQPGGYRVLEDLGLKDAVEDiDAQVVDGYIIHDQ 199
Cdd:PRK07333    4 VVIAGGGYVGLALAVAL-KQAAphlPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAP-EAQPITDMVITDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952977115 200 DSKSEVQiPYPVSENSQVRSGRAFHH----GRFIMGLRKAAMAEpNTKFIEGIVLQLLEEDDAVMGVQYRDKETgdvkeL 275
Cdd:PRK07333   82 RTSDPVR-PVFLTFEGEVEPGEPFAHmvenRVLINALRKRAEAL-GIDLREATSVTDFETRDEGVTVTLSDGSV-----L 154

                         170
                  ....*....|....*..
gi 1952977115 276 HAPLTVVADGLFSKFRK 292
Cdd:PRK07333  155 EARLLVAADGARSKLRE 171
 
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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