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Conserved domains on  [gi|6324932|ref|NP_015001|]
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putative electron-transferring-flavoprotein dehydrogenase [Saccharomyces cerevisiae S288C]

Protein Classification

electron transfer flavoprotein-ubiquinone oxidoreductase( domain architecture ID 11428947)

electron transfer flavoprotein-ubiquinone oxidoreductase accepts electrons from ETF and reduces ubiquinone

CATH:  3.30.70.20|3.30.9.90|3.50.50.60
EC:  1.5.5.1
Gene Ontology:  GO:0004174|GO:0022900|GO:0046872|GO:0051539
SCOP:  4000064|4000127

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ETF_QO pfam05187
Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer ...
 523-629 2.48e-67

Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64-kDa monomer.


:

Pssm-ID: 461576 [Multi-domain]  Cd Length: 104  Bit Score: 214.79  E-value: 2.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    523 GVISFDILTSVSRTGTYHDDDEPCHLRVPgqDMVKYAERSFPVWKGVESRFCPAGVYEFVKDEkSPVGTRLQINSQNCIH 602
Cdd:pfam05187   1 GVLTFDRLTSVYLSGTNHEEDQPCHLKLK--DPEVPIKVNLPKYAGPEQRYCPAGVYEYVEDE-EPGGPRLQINAQNCVH 77

                          90       100
                  ....*....|....*....|....*..
gi 6324932    603 CKTCDIKAPRQDITWKVPEGGDGPKYT 629
Cdd:pfam05187  78 CKTCDIKDPTQNITWVVPEGGGGPNYP 104
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
70-451 1.30e-49

Dehydrogenase (flavoprotein) [Energy production and conversion];


:

Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 174.00  E-value: 1.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   70 GGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTVSGAILePGVWKELFPdeksdigIPLPKELATLVTKEHLKF 149
Cdd:COG0644   1 AGPAGSAAARRLARAG-------LSVLLLEKGSFPGDKICGGGLL-PRALEELEP-------LGLDEPLERPVRGARFYS 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  150 LKGKwAISVPEPsqminKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVkgVITKDagisksgkpket 229
Cdd:COG0644  66 PGGK-SVELPPG-----RGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV--VRTGD------------ 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  230 ferGMEFWARQTVLAEGCHGSLTKQALAKydlRKGRQHQTYGLGIKEVWEVKP-ENFNKGFAAHTMGYPLTNdvyGGGFQ 308
Cdd:COG0644 126 ---GEEIRADYVVDADGARSLLARKLGLK---RRSDEPQDYALAIKEHWELPPlEGVDPGAVEFFFGEGAPG---GYGWV 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  309 YHFGDGLVTVGLVVGldyknpyvspykefqkmkhhpyyskvleggkciayaaralnegglQSVPKLNFPGGVLVGASAGF 388
Cdd:COG0644 197 FPLGDGRVSVGIPLG---------------------------------------------GPRPRLVGDGVLLVGDAAGF 231

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324932  389 MNVPKIKGTHTAMKSGLLAAESIFESIKGLPVLEEvededakmamfdkeatiNLESYESAFKE 451
Cdd:COG0644 232 VDPLTGEGIHLAMKSGRLAAEAIAEALEGGDFSAE-----------------ALAEYERRLRE 277
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 46-78 4.82e-03

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 PLN02463:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 447  Bit Score: 39.70  E-value: 4.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 6324932    46 LTEEEKELLN------EPRARDYVDVCIVGGGPAGLATA 78
Cdd:PLN02463   6 VPETKKENLDfelprfDPSKSRVVDLVVVGGGPAGLAVA 44
 
Name Accession Description Interval E-value
ETF_QO pfam05187
Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer ...
 523-629 2.48e-67

Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64-kDa monomer.


Pssm-ID: 461576 [Multi-domain]  Cd Length: 104  Bit Score: 214.79  E-value: 2.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    523 GVISFDILTSVSRTGTYHDDDEPCHLRVPgqDMVKYAERSFPVWKGVESRFCPAGVYEFVKDEkSPVGTRLQINSQNCIH 602
Cdd:pfam05187   1 GVLTFDRLTSVYLSGTNHEEDQPCHLKLK--DPEVPIKVNLPKYAGPEQRYCPAGVYEYVEDE-EPGGPRLQINAQNCVH 77

                          90       100
                  ....*....|....*....|....*..
gi 6324932    603 CKTCDIKAPRQDITWKVPEGGDGPKYT 629
Cdd:pfam05187  78 CKTCDIKDPTQNITWVVPEGGGGPNYP 104
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
70-451 1.30e-49

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 174.00  E-value: 1.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   70 GGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTVSGAILePGVWKELFPdeksdigIPLPKELATLVTKEHLKF 149
Cdd:COG0644   1 AGPAGSAAARRLARAG-------LSVLLLEKGSFPGDKICGGGLL-PRALEELEP-------LGLDEPLERPVRGARFYS 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  150 LKGKwAISVPEPsqminKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVkgVITKDagisksgkpket 229
Cdd:COG0644  66 PGGK-SVELPPG-----RGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV--VRTGD------------ 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  230 ferGMEFWARQTVLAEGCHGSLTKQALAKydlRKGRQHQTYGLGIKEVWEVKP-ENFNKGFAAHTMGYPLTNdvyGGGFQ 308
Cdd:COG0644 126 ---GEEIRADYVVDADGARSLLARKLGLK---RRSDEPQDYALAIKEHWELPPlEGVDPGAVEFFFGEGAPG---GYGWV 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  309 YHFGDGLVTVGLVVGldyknpyvspykefqkmkhhpyyskvleggkciayaaralnegglQSVPKLNFPGGVLVGASAGF 388
Cdd:COG0644 197 FPLGDGRVSVGIPLG---------------------------------------------GPRPRLVGDGVLLVGDAAGF 231

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324932  389 MNVPKIKGTHTAMKSGLLAAESIFESIKGLPVLEEvededakmamfdkeatiNLESYESAFKE 451
Cdd:COG0644 232 VDPLTGEGIHLAMKSGRLAAEAIAEALEGGDFSAE-----------------ALAEYERRLRE 277
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
533-628 1.15e-28

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 109.14  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  533 VSRTGTYHDDDEPcHLRVPGQDMVKYAERSFPvwkgvESRFCPAGVYEFVKDEkspvgtRLQINSQNCIHCKTCDIKAPR 612
Cdd:COG2440   1 LFLNNYNVDEDQP-HIKVKDPDICIARCLAKP-----CTRYCPAGVYEIVGDG------RLQINYENCLECGTCRIKCPT 68

                        90
                ....*....|....*.
gi 6324932  613 QDITWKVPEGGDGPKY 628
Cdd:COG2440  69 QNITWVYPEGGGGVNY 84
PRK10015 PRK10015
oxidoreductase; Provisional
 61-464 4.48e-24

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 105.44  E-value: 4.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    61 DYVDVCIVGGGPAGLATAIKLKQldnssgtGQLRVVVLEKSSVLGGQTVSGAILEPGVWKELFPdeksdiGIPLPKELAT 140
Cdd:PRK10015   4 DKFDAIVVGAGVAGSVAALVMAR-------AGLDVLVIERGDSAGCKNMTGGRLYAHTLEAIIP------GFAASAPVER 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   141 LVTKEHLKFLKGKWAISVP---EPSQMINKGrNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVsDLIYDENNAVKGVITKD 217
Cdd:PRK10015  71 KVTREKISFLTEESAVTLDfhrEQPDVPQHA-SYTVLRNRLDPWLMEQAEQAGAQFIPGVRV-DALVREGNKVTGVQAGD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   218 agisksgkpkETFErgmefwARQTVLAEGCHGSLTKQalakYDLRKGRQHQTYGLGIKEVWEVKPENFNKGF--AAHT-- 293
Cdd:PRK10015 149 ----------DILE------ANVVILADGVNSMLGRS----LGMVPASDPHHYAVGVKEVIGLTPEQINDRFniTGEEga 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   294 ----MGYPlTNDVYGGGFQYHFGDGlVTVGLVVGL-DYKNPYVSPYKEFQKMKHHPYYSKVLEGGKCIAYAARALNEGGL 368
Cdd:PRK10015 209 awlfAGSP-SDGLMGGGFLYTNKDS-ISLGLVCGLgDIAHAQKSVPQMLEDFKQHPAIRPLISGGKLLEYSAHMVPEGGL 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   369 QSVPKLNFPGGVLVGASAGF-MNVP-KIKGTHTAMKSGLLAAESIFESikglpvlEEVEDEDAKmamfdkeatiNLESYE 446
Cdd:PRK10015 287 AMVPQLVNDGVMIVGDAAGFcLNLGfTVRGMDLAIASAQAAATTVIAA-------KERADFSAS----------SLAQYK 349

                        410
                 ....*....|....*...
gi 6324932   447 SAFKESSIYKELYEVRNI 464
Cdd:PRK10015 350 RELEQSCVMRDMQHFRKI 367
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 64-411 2.59e-10

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 61.95  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     64 DVCIVGGGPAGLATAIKLKQldnssgTGqLRVVVLEKSSVLGGQTVSGAIlEPGVWKELfpdeksdigiPLPKELATLVT 143
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLAD------KG-LRVLLLEKKSFPRYKPCGGAL-SPRALEEL----------DLPGELIVNLV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    144 KEHLKFLKGKWAISVPEPSqminkGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVKGVITkdagisks 223
Cdd:TIGR02032  64 RGARFFSPNGDSVEIPIET-----ELAYVIDRDAFDEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRG-------- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    224 gkpketfeRGMEFWARQTVLAEGCHGSLTKqalaKYDLRKgrQHQTYGLGIKEVWEVKPENFNKGFAahTMGYPLtnDVY 303
Cdd:TIGR02032 131 --------SEGTVTAKIVIGADGSRSIVAK----KLGLKK--EPREYGVAARAEVEMPDEEVDEDFV--EVYIDR--GIV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    304 GGGFQYHF--GDGLVTVGLVVGLDYKnpYVSPYKEFQK-MKHHPYYSKVLEGGKCIAYAARAlneGGLQSVPKLNFpggV 380
Cdd:TIGR02032 193 PGGYGWVFpkGDGTANVGVGSRSAEE--GEDPKKYLKDfLARRPELKDAETVEVCGALIPIG---RPDEKLVRGNV---L 264

                         330       340       350
                  ....*....|....*....|....*....|.
gi 6324932    381 LVGASAGFMNVPKIKGTHTAMKSGLLAAESI 411
Cdd:TIGR02032 265 LVGDAAGHVNPLTGEGIYYAMRSGDIAAEVV 295
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 64-112 2.46e-06

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 50.30  E-value: 2.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLdnssGtgqLRVVVLEKSSVLGGQTVSGA 112
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARA----G---AKVLLVERRGFLGGMLTSGL 42
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 564-611 1.30e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 38.55  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324932   564 PVWKGvESR---------FCPAGVYEFVKDEKSPVGTRLQINS-QNCIHCKTCDIKAP 611
Cdd:PRK09626  10 PVWVD-ESRckacdicvsVCPAGVLAMRIDPHAVLGKMIKVVHpESCIGCRECELHCP 66
PLN02463 PLN02463
lycopene beta cyclase
 46-78 4.82e-03

lycopene beta cyclase


Pssm-ID: 178082 [Multi-domain]  Cd Length: 447  Bit Score: 39.70  E-value: 4.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 6324932    46 LTEEEKELLN------EPRARDYVDVCIVGGGPAGLATA 78
Cdd:PLN02463   6 VPETKKENLDfelprfDPSKSRVVDLVVVGGGPAGLAVA 44
 
Name Accession Description Interval E-value
ETF_QO pfam05187
Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer ...
 523-629 2.48e-67

Electron transfer flavoprotein-ubiquinone oxidoreductase, 4Fe-4S; Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64-kDa monomer.


Pssm-ID: 461576 [Multi-domain]  Cd Length: 104  Bit Score: 214.79  E-value: 2.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    523 GVISFDILTSVSRTGTYHDDDEPCHLRVPgqDMVKYAERSFPVWKGVESRFCPAGVYEFVKDEkSPVGTRLQINSQNCIH 602
Cdd:pfam05187   1 GVLTFDRLTSVYLSGTNHEEDQPCHLKLK--DPEVPIKVNLPKYAGPEQRYCPAGVYEYVEDE-EPGGPRLQINAQNCVH 77

                          90       100
                  ....*....|....*....|....*..
gi 6324932    603 CKTCDIKAPRQDITWKVPEGGDGPKYT 629
Cdd:pfam05187  78 CKTCDIKDPTQNITWVVPEGGGGPNYP 104
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
70-451 1.30e-49

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 174.00  E-value: 1.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   70 GGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTVSGAILePGVWKELFPdeksdigIPLPKELATLVTKEHLKF 149
Cdd:COG0644   1 AGPAGSAAARRLARAG-------LSVLLLEKGSFPGDKICGGGLL-PRALEELEP-------LGLDEPLERPVRGARFYS 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  150 LKGKwAISVPEPsqminKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVkgVITKDagisksgkpket 229
Cdd:COG0644  66 PGGK-SVELPPG-----RGGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV--VRTGD------------ 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  230 ferGMEFWARQTVLAEGCHGSLTKQALAKydlRKGRQHQTYGLGIKEVWEVKP-ENFNKGFAAHTMGYPLTNdvyGGGFQ 308
Cdd:COG0644 126 ---GEEIRADYVVDADGARSLLARKLGLK---RRSDEPQDYALAIKEHWELPPlEGVDPGAVEFFFGEGAPG---GYGWV 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  309 YHFGDGLVTVGLVVGldyknpyvspykefqkmkhhpyyskvleggkciayaaralnegglQSVPKLNFPGGVLVGASAGF 388
Cdd:COG0644 197 FPLGDGRVSVGIPLG---------------------------------------------GPRPRLVGDGVLLVGDAAGF 231

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324932  389 MNVPKIKGTHTAMKSGLLAAESIFESIKGLPVLEEvededakmamfdkeatiNLESYESAFKE 451
Cdd:COG0644 232 VDPLTGEGIHLAMKSGRLAAEAIAEALEGGDFSAE-----------------ALAEYERRLRE 277
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
533-628 1.15e-28

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 109.14  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  533 VSRTGTYHDDDEPcHLRVPGQDMVKYAERSFPvwkgvESRFCPAGVYEFVKDEkspvgtRLQINSQNCIHCKTCDIKAPR 612
Cdd:COG2440   1 LFLNNYNVDEDQP-HIKVKDPDICIARCLAKP-----CTRYCPAGVYEIVGDG------RLQINYENCLECGTCRIKCPT 68

                        90
                ....*....|....*.
gi 6324932  613 QDITWKVPEGGDGPKY 628
Cdd:COG2440  69 QNITWVYPEGGGGVNY 84
PRK10015 PRK10015
oxidoreductase; Provisional
 61-464 4.48e-24

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 105.44  E-value: 4.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    61 DYVDVCIVGGGPAGLATAIKLKQldnssgtGQLRVVVLEKSSVLGGQTVSGAILEPGVWKELFPdeksdiGIPLPKELAT 140
Cdd:PRK10015   4 DKFDAIVVGAGVAGSVAALVMAR-------AGLDVLVIERGDSAGCKNMTGGRLYAHTLEAIIP------GFAASAPVER 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   141 LVTKEHLKFLKGKWAISVP---EPSQMINKGrNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVsDLIYDENNAVKGVITKD 217
Cdd:PRK10015  71 KVTREKISFLTEESAVTLDfhrEQPDVPQHA-SYTVLRNRLDPWLMEQAEQAGAQFIPGVRV-DALVREGNKVTGVQAGD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   218 agisksgkpkETFErgmefwARQTVLAEGCHGSLTKQalakYDLRKGRQHQTYGLGIKEVWEVKPENFNKGF--AAHT-- 293
Cdd:PRK10015 149 ----------DILE------ANVVILADGVNSMLGRS----LGMVPASDPHHYAVGVKEVIGLTPEQINDRFniTGEEga 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   294 ----MGYPlTNDVYGGGFQYHFGDGlVTVGLVVGL-DYKNPYVSPYKEFQKMKHHPYYSKVLEGGKCIAYAARALNEGGL 368
Cdd:PRK10015 209 awlfAGSP-SDGLMGGGFLYTNKDS-ISLGLVCGLgDIAHAQKSVPQMLEDFKQHPAIRPLISGGKLLEYSAHMVPEGGL 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   369 QSVPKLNFPGGVLVGASAGF-MNVP-KIKGTHTAMKSGLLAAESIFESikglpvlEEVEDEDAKmamfdkeatiNLESYE 446
Cdd:PRK10015 287 AMVPQLVNDGVMIVGDAAGFcLNLGfTVRGMDLAIASAQAAATTVIAA-------KERADFSAS----------SLAQYK 349

                        410
                 ....*....|....*...
gi 6324932   447 SAFKESSIYKELYEVRNI 464
Cdd:PRK10015 350 RELEQSCVMRDMQHFRKI 367
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 59-416 2.86e-20

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 93.82  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    59 ARDYVDVCIVGGGPAGLATAIKLKQldnsSGTgqlRVVVLEKSSVLGGQTVSGAILEPGVWKELFPdeksdiGIPLPKEL 138
Cdd:PRK10157   2 SEDIFDAIIVGAGLAGSVAALVLAR----EGA---QVLVIERGNSAGAKNVTGGRLYAHSLEHIIP------GFADSAPV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   139 ATLVTKEHLKFL--KGKWAISVPEPSQMINKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVkgvitk 216
Cdd:PRK10157  69 ERLITHEKLAFMteKSAMTMDYCNGDETSPSQRSYSVLRSKFDAWLMEQAEEAGAQLITGIRVDNLVQRDGKVV------ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   217 daGISKSGKPKEtfergmefwARQTVLAEGCHGSLTKqalaKYDLRKGRQHQTYGLGIKEVWEVkPENF---------NK 287
Cdd:PRK10157 143 --GVEADGDVIE---------AKTVILADGVNSILAE----KLGMAKRVKPTDVAVGVKELIEL-PKSViedrfqlqgNQ 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   288 GFAAHTMGYPlTNDVYGGGFQYHfGDGLVTVGLVVGLDY-KNPYVSPYKEFQKMKHHPYYSKVLEGGKCIAYAARALNEG 366
Cdd:PRK10157 207 GAACLFAGSP-TDGLMGGGFLYT-NENTLSLGLVCGLHHlHDAKKSVPQMLEDFKQHPAVAPLIAGGKLVEYSAHVVPEA 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6324932   367 GLQSVPKLNFPGGVLVGASAGF-MNVP-KIKGTHTAMKSGLLAAESIFESIK 416
Cdd:PRK10157 285 GINMLPELVGDGVLIAGDAAGMcMNLGfTIRGMDLAIAAGEAAAKTVLSAMK 336
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 63-246 1.20e-10

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 64.08  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTV--SGAILEPGVWKELFPDEKS------DI---- 130
Cdd:COG1053   4 YDVVVVGSGGAGLRAALEAAEAG-------LKVLVLEKVPPRGGHTAaaQGGINAAGTNVQKAAGEDSpeehfyDTvkgg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  131 -GIPLPKELATLVTK--EHLKFLKgkwAISVP---EPSQMIN------KGRNYIVSL---NQVVGYLGEKAEEVGVEVYP 195
Cdd:COG1053  77 dGLADQDLVEALAEEapEAIDWLE---AQGVPfsrTPDGRLPqfgghsVGRTCYAGDgtgHALLATLYQAALRLGVEIFT 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324932  196 GIAVSDLIYDeNNAVKGVITKDagisKSGKPKetfergmEFWARQTVLAEG 246
Cdd:COG1053 154 ETEVLDLIVD-DGRVVGVVARD----RTGEIV-------RIRAKAVVLATG 192
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 64-411 2.59e-10

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 61.95  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     64 DVCIVGGGPAGLATAIKLKQldnssgTGqLRVVVLEKSSVLGGQTVSGAIlEPGVWKELfpdeksdigiPLPKELATLVT 143
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLAD------KG-LRVLLLEKKSFPRYKPCGGAL-SPRALEEL----------DLPGELIVNLV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    144 KEHLKFLKGKWAISVPEPSqminkGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVKGVITkdagisks 223
Cdd:TIGR02032  64 RGARFFSPNGDSVEIPIET-----ELAYVIDRDAFDEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRG-------- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    224 gkpketfeRGMEFWARQTVLAEGCHGSLTKqalaKYDLRKgrQHQTYGLGIKEVWEVKPENFNKGFAahTMGYPLtnDVY 303
Cdd:TIGR02032 131 --------SEGTVTAKIVIGADGSRSIVAK----KLGLKK--EPREYGVAARAEVEMPDEEVDEDFV--EVYIDR--GIV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    304 GGGFQYHF--GDGLVTVGLVVGLDYKnpYVSPYKEFQK-MKHHPYYSKVLEGGKCIAYAARAlneGGLQSVPKLNFpggV 380
Cdd:TIGR02032 193 PGGYGWVFpkGDGTANVGVGSRSAEE--GEDPKKYLKDfLARRPELKDAETVEVCGALIPIG---RPDEKLVRGNV---L 264

                         330       340       350
                  ....*....|....*....|....*....|.
gi 6324932    381 LVGASAGFMNVPKIKGTHTAMKSGLLAAESI 411
Cdd:TIGR02032 265 LVGDAAGHVNPLTGEGIYYAMRSGDIAAEVV 295
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 57-106 3.25e-08

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: 56.02  E-value: 3.25e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6324932   57 PRARDYVDVCIVGGGPAGLATAIKLKQLdnssgtgQLRVVVLEKSSVLGG 106
Cdd:COG2072   1 TAATEHVDVVVIGAGQAGLAAAYHLRRA-------GIDFVVLEKADDVGG 43
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 63-207 2.00e-07

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: 53.40  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTVSGAILEP--------GVWKELfpdekSDIGIPL 134
Cdd:COG0654   4 TDVLIVGGGPAGLALALALARAG-------IRVTVVERAPPPRPDGRGIALSPRslellrrlGLWDRL-----LARGAPI 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324932  135 PKelATLVTKEHlkflkGKWAISVPEPSQMINKGrnYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDEN 207
Cdd:COG0654  72 RG--IRVRDGSD-----GRVLARFDAAETGLPAG--LVVPRADLERALLEAARALGVELRFGTEVTGLEQDAD 135
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 63-156 4.60e-07

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: 52.53  E-value: 4.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGG----QTVSGAILEPG-------------VWKEL-FP 124
Cdd:COG1232   2 KRVAVIGGGIAGLTAAYRLAKAG-------HEVTVLEASDRVGGlirtVEVDGFRIDRGphsfltrdpevleLLRELgLG 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6324932  125 DE-------KSDI---G--IPLPKELATLVTKEHLKfLKGKWAI 156
Cdd:COG1232  75 DElvwpntrKSYIyygGklHPLPQGPLALLRSPLLS-LAGKLRA 117
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
63-267 1.40e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 50.67  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQT-VSGAILEPGV------------------WKELF 123
Cdd:COG0665   3 ADVVVIGGGIAGLSTAYHLARRG-------LDVTVLERGRPGSGASgRNAGQLRPGLaaladralvrlarealdlWRELA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  124 PDEKSDIGIPLPKELATLVTKEHLKFLKGKWAI--SVPEPSQMIN----KGRNYIVSLNQVVGY---------------- 181
Cdd:COG0665  76 AELGIDCDFRRTGVLYLARTEAELAALRAEAEAlrALGLPVELLDaaelREREPGLGSPDYAGGlydpddghvdpaklvr 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  182 -LGEKAEEVGVEVYPGIAVSDLIYdENNAVKGVITkdagisksgkPKETFErgmefwARQTVLAEGCH-GSLTKQALAKY 259
Cdd:COG0665 156 aLARAARAAGVRIREGTPVTGLER-EGGRVTGVRT----------ERGTVR------ADAVVLAAGAWsARLLPMLGLRL 218


                ....*...
gi 6324932  260 DLRKGRQH 267
Cdd:COG0665 219 PLRPVRGY 226
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 64-112 2.46e-06

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 50.30  E-value: 2.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLdnssGtgqLRVVVLEKSSVLGGQTVSGA 112
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARA----G---AKVLLVERRGFLGGMLTSGL 42
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 64-106 8.75e-06

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 48.69  E-value: 8.75e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6324932   64 DVCIVGGGPAGLATAIKLKQldnsSGtgqLRVVVLEKSSVLGG 106
Cdd:COG1233   5 DVVVIGAGIGGLAAAALLAR----AG---YRVTVLEKNDTPGG 40
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 63-114 1.40e-05

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 48.15  E-value: 1.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6324932    63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQT-VSGAIL 114
Cdd:PRK12842  10 CDVLVIGSGAGGLSAAITARKLG-------LDVVVLEKEPVFGGTTaFSGGVL 55
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
58-122 1.52e-05

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 47.61  E-value: 1.52e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324932   58 RARDYVDVCIVGGGPAGLATAIKLKQLdnssGtgqLRVVVLEKSSVLGGQTVSGAILEPGVWKEL 122
Cdd:COG1231   3 RRARGKDVVIVGAGLAGLAAARELRKA----G---LDVTVLEARDRVGGRVWTLRFGDDGLYAEL 60
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
64-107 1.76e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 47.04  E-value: 1.76e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6324932   64 DVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSvLGGQ 107
Cdd:COG0492   2 DVVIIGAGPAGLTAAIYAARAG-------LKTLVIEGGE-PGGQ 37
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 64-246 3.08e-05

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 46.51  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     64 DVCIVGGGPAGLATAIKLKQldnssgtGQLRVVVLEKSSVLGGQTV--SGAI---------------------------L 114
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAE-------AGLKVAVVEKGQPFGGATAwsSGGIdalgnppqggidspelhptdtlkgldeL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    115 EPGVWKELFPDEKSDI-------GIPLPKELATLVTKEHLKFLKGKWAIsvpePSQMINKGRNyIVSLNQVVGYLGEKAE 187
Cdd:pfam00890  74 ADHPYVEAFVEAAPEAvdwlealGVPFSRTEDGHLDLRPLGGLSATWRT----PHDAADRRRG-LGTGHALLARLLEGLR 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324932    188 EVGVEVYPGIAVSDLIYdENNAVKGVItkdAGISKSGKPKETFERgmefwaRQTVLAEG 246
Cdd:pfam00890 149 KAGVDFQPRTAADDLIV-EDGRVTGAV---VENRRNGREVRIRAI------AAVLLATG 197
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 64-118 3.23e-05

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: 46.62  E-value: 3.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQT--VSGAILEPGV 118
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRG-------LSVTLLERGDDPGSGAsgRNAGLIHPGL 50
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
67-113 3.98e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 41.75  E-value: 3.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6324932     67 IVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQTVSGAI 113
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRG-------FRVLVLEKRDRLGGNAYSYRV 40
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
64-106 9.71e-05

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 44.87  E-value: 9.71e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6324932   64 DVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGG 106
Cdd:COG3380   5 DIAIIGAGIAGLAAARALQDAG-------HEVTVFEKSRGVGG 40
PRK09126 PRK09126
FAD-dependent hydroxylase;
63-128 1.14e-04

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 44.93  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324932    63 VDVCIVGGGPAGLATAIKLKQLdnssgtgQLRVVVLEKSS--VLGGQTVSG----------AILEP-GVWKELFPDEKS 128
Cdd:PRK09126   4 SDIVVVGAGPAGLSFARSLAGS-------GLKVTLIERQPlaALADPAFDGreialthasrEILQRlGAWDRIPEDEIS 75
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
61-108 2.08e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 43.98  E-value: 2.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6324932   61 DYVDVCIVGGGPAGLATAIKLKQLDNssgtgqLRVVVLEK-SSVLGGQT 108
Cdd:COG0579   3 EMYDVVIIGAGIVGLALARELSRYED------LKVLVLEKeDDVAQESS 45
PRK07208 PRK07208
hypothetical protein; Provisional
 63-126 3.47e-04

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 43.34  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGG--QTVS--GAILEPG-------------VWKELFPD 125
Cdd:PRK07208   5 KSVVIIGAGPAGLTAAYELLKRG-------YPVTVLEADPVVGGisRTVTykGNRFDIGghrffskspevmdLWNEILPD 77


                 .
gi 6324932   126 E 126
Cdd:PRK07208  78 D 78
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 63-114 4.81e-04

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 43.20  E-value: 4.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6324932    63 VDVCIVGGGPAGLATAIKLKqldnSSGtgqLRVVVLEKSSVLGGQT-VSGAIL 114
Cdd:PRK12844   7 YDVVVVGSGGGGMCAALAAA----DSG---LEPLIVEKQDKVGGSTaMSGGVL 52
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 59-106 5.26e-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: 42.77  E-value: 5.26e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6324932   59 ARDYvDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKsSVLGG 106
Cdd:COG1249   1 MKDY-DLVVIGAGPGGYVAAIRAAQLG-------LKVALVEK-GRLGG 39
PRK07233 PRK07233
hypothetical protein; Provisional
 65-106 5.54e-04

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 42.95  E-value: 5.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6324932    65 VCIVGGGPAGLATAIKLkqldnsSGTGQlRVVVLEKSSVLGG 106
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRL------AKRGH-EVTVFEADDQLGG 36
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 64-106 5.60e-04

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 42.92  E-value: 5.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6324932   64 DVCIVGGGPAGLATAIKLkqldnsSGTGqLRVVVLEKSSVLGG 106
Cdd:COG3349   5 RVVVVGGGLAGLAAAVEL------AEAG-FRVTLLEARPRLGG 40
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 564-611 1.30e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 38.55  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324932   564 PVWKGvESR---------FCPAGVYEFVKDEKSPVGTRLQINS-QNCIHCKTCDIKAP 611
Cdd:PRK09626  10 PVWVD-ESRckacdicvsVCPAGVLAMRIDPHAVLGKMIKVVHpESCIGCRECELHCP 66
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
64-105 1.30e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 41.48  E-value: 1.30e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 6324932   64 DVCIVGGGPAGLATAIKLKQLdnssGTGQLRVVVLEKSSVLG 105
Cdd:COG4529   7 RIAIIGGGASGTALAIHLLRR----APEPLRITLFEPRPELG 44
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 62-255 1.34e-03

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: 41.54  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     62 YVDVCIVGGGPAGLATAIKLkqldnssGTGQLRVVVLEKSSVLgGQTVSGAILEP---------GVWKELFPDeksdigi 132
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLL-------ARAGVRVVLVERHATT-SVLPRAHGLNQrtmellrqaGLEDRILAE------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932    133 PLPKELATLVT-----KEHLKFLkgkwaiSVPEPSQMINKgrnyivslNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDEN 207
Cdd:pfam01494  66 GVPHEGMGLAFyntrrRADLDFL------TSPPRVTVYPQ--------TELEPILVEHAEARGAQVRFGTEVLSLEQDGD 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 6324932    208 NaVKGVITkdagiSKSGKPKETFErgmefwARQTVLAEGCHGSLTKQA 255
Cdd:pfam01494 132 G-VTAVVR-----DRRDGEEYTVR------AKYLVGCDGGRSPVRKTL 167
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 64-130 1.68e-03

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 41.03  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLdnssgtgQLRVVVLEK-------SSVLGGQTV-----SGAILEP-GVWKELFPDEKSDI 130
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARS-------GLKVALIEAtplpapaDPGFDNRVSalsaaSIRLLEKlGVWDKIEPARAQPI 73
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 65-109 1.76e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 41.37  E-value: 1.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6324932    65 VCIVGGGPAGLATAIKLKQLDnssgtGQLRVVVLEKSSVLGG--QTV 109
Cdd:PRK11883   3 VAIIGGGITGLSAAYRLHKKG-----PDADITLLEASDRLGGkiQTV 44
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 64-180 1.86e-03

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: 40.76  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLdnssgtgQLRVVVLEKSSVLGGQtvsGAILEPGVWKELFPDEKSDIGIPLPKELATLVT 143
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQL-------GGKVTLIEDEGTCPYG---GCVLSKALLGAAEAPEIASLWADLYKRKEEVVK 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6324932    144 K--EHLKFLKGKWAISvpepsqmINKGRNYIVSLNQVVG 180
Cdd:pfam07992  72 KlnNGIEVLLGTEVVS-------IDPGAKKVVLEELVDG 103
PRK08275 PRK08275
putative oxidoreductase; Provisional
 64-113 2.64e-03

putative oxidoreductase; Provisional


Pssm-ID: 181346 [Multi-domain]  Cd Length: 554  Bit Score: 40.81  E-value: 2.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 6324932    64 DVCIVGGGPAGLATAIKLKQLDNSsgtgqLRVVVLEKSSVlggqTVSGAI 113
Cdd:PRK08275  11 DILVIGGGTAGPMAAIKAKERNPA-----LRVLLLEKANV----KRSGAI 51
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
50-107 4.24e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.23  E-value: 4.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324932   50 EKELLNEPRARDYVDVC----IVGGGPAGLATAIKLkqldnsSGTGqLRVVVLEKSSVLGGQ 107
Cdd:COG1148 124 AKAKLLEPLEPIKVPVNkralVIGGGIAGMTAALEL------AEQG-YEVYLVEKEPELGGR 178
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 63-108 4.29e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 40.09  E-value: 4.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 6324932    63 VDVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGGQT 108
Cdd:PRK06134  13 CDVLVIGSGAAGLSAAVTAAWHG-------LKVIVVEKDPVFGGTT 51
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
64-246 4.66e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 39.71  E-value: 4.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932   64 DVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEK-----------------------SSVLGGqtVSGAIlepgvwk 120
Cdd:COG2509  32 DVVIVGAGPAGLFAALELAEAG-------LKPLVLERgkdveertcpvaefwrkgkcnpeSNIQFG--EGGAG------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324932  121 eLFPDEKSDIGIPLPKELATLVTKEHLKFlkGkwA----ISVPEP-------SQMINKGRNYIVSLnqvvgylgekaeev 189
Cdd:COG2509  96 -TFSDGKLNTRSKDPQGLIRYVLEIFVKF--G--ApeeiLYAAKPhigtdklPKVVKNIREYIEEL-------------- 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324932  190 GVEVYPGIAVSDLIYdENNAVKGVITKDagisksgkpketferGMEFWARQTVLAEG 246
Cdd:COG2509 157 GGEIRFNTRVTDILI-EDGRVKGVVTND---------------GEEIEADAVILAPG 197
PLN02463 PLN02463
lycopene beta cyclase
 46-78 4.82e-03

lycopene beta cyclase


Pssm-ID: 178082 [Multi-domain]  Cd Length: 447  Bit Score: 39.70  E-value: 4.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 6324932    46 LTEEEKELLN------EPRARDYVDVCIVGGGPAGLATA 78
Cdd:PLN02463   6 VPETKKENLDfelprfDPSKSRVVDLVVVGGGPAGLAVA 44
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 65-106 5.60e-03

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 39.73  E-value: 5.60e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6324932   65 VCIVGGGPAGLATAiklkqldnssgtGQLR-----VVVLEKSSVLGG 106
Cdd:COG0493 124 VAVVGSGPAGLAAA------------YQLAragheVTVFEALDKPGG 158
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
64-113 6.38e-03

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 39.42  E-value: 6.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6324932    64 DVCIVGGGPAGLATAIKLKQLdnssgTGQLRVVVLEKSSVLGG-QT--VSGAI 113
Cdd:PRK11728   4 DFVIIGGGIVGLSTAMQLQER-----YPGARIAVLEKESGPARhQTghNSGVI 51
carotene-cycl TIGR01790
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ...
 64-106 6.85e-03

lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.


Pssm-ID: 130850 [Multi-domain]  Cd Length: 388  Bit Score: 39.34  E-value: 6.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6324932     64 DVCIVGGGPAGLATAIKLKQLDnssgtgqLRVVVLEKSSVLGG 106
Cdd:TIGR01790   1 DLAVIGGGPAGLAIALELARPG-------LRVQLIEPHPPIPG 36
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 64-108 9.93e-03

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 38.93  E-value: 9.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6324932   64 DVCIVGGGPAGLATAIKLKQldnssgtgQLRVVVLEKSSVLGGQT 108
Cdd:COG0029   6 DVLVIGSGIAGLSAALKLAE--------RGRVTLLTKGELGESNT 42
 
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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