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Conserved domains on  [gi|504816830|ref|WP_015003932|]
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NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia phenoliruptrix]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11457516)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
99-536 0e+00

FAD-dependent dehydrogenase [General function prediction only];


:

Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 752.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  99 TAPRPVVIGMGPCGLFAGLILAQMGFRPIILERGKAVRERTKDTFGLWRKSVLNPESNVQFGEGGAGTFSDGKLYSQIKD 178
Cdd:COG2509   29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDVEERTCPVAEFWRKGKCNPESNIQFGEGGAGTFSDGKLNTRSKD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 179 PKHYGRKVLDEFVRAGAPEDILYLSRPHIGTFRLVSMVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTGETLR 258
Cdd:COG2509  109 PQGLIRYVLEIFVKFGAPEEILYAAKPHIGTDKLPKVVKNIREYIEELGGEIRFNTRVTDILIEDGRVKGVVTNDGEEIE 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 259 CDHVVLAVGHSARDTFQMLHDRGVYIEAKPFSLGFRIEHPQGVIDRSRFGKFAGHKQLGAADYKVVHHCSN-GRAVYSFC 337
Cdd:COG2509  189 ADAVILAPGHSARDWFEMLHRLGVKLEAKPFDIGVRVEHPQELIDRIQYGKFAGHPLLGAAEYKLVYQTKNyGRGVYTFC 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 338 MCPGGTVVAATSEPGRVVTNGMSQYSRAERNANAGIVVGITPDDYPGGPLAGIAFQRKWEERAFELGGGNYMAPGQLVGD 417
Cdd:COG2509  269 MCPGGFVVAEASEPGLVVVNGMSYSDRKSENANFALLVSVTPTDFPGGPLAGIEYQRSIERLANELGGGNYKAPAQRLGD 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 418 FIAGRPSTSLGSVVPSYKPGVHPTDLSTALPDYVIEAIREALPQLEKKIAGFAMHDAVLTGVETRTSSPIRVRRRDDYQS 497
Cdd:COG2509  349 FLAGRRSTELGSVEPTYKPGVTPGDLSLVLPYRILDALREALEAFDKKIPGFASDDALLYGVETRTSSPVRIPRDEDLET 428

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 504816830 498 mNVEGLYPagegagyaggIYSAAIDGIEVAEAVALKMTG 536
Cdd:COG2509  429 -NIKGLYPagegagyaggIVSAAVDGIRVAEAIAEKLGP 466
 
Name Accession Description Interval E-value
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
99-536 0e+00

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 752.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  99 TAPRPVVIGMGPCGLFAGLILAQMGFRPIILERGKAVRERTKDTFGLWRKSVLNPESNVQFGEGGAGTFSDGKLYSQIKD 178
Cdd:COG2509   29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDVEERTCPVAEFWRKGKCNPESNIQFGEGGAGTFSDGKLNTRSKD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 179 PKHYGRKVLDEFVRAGAPEDILYLSRPHIGTFRLVSMVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTGETLR 258
Cdd:COG2509  109 PQGLIRYVLEIFVKFGAPEEILYAAKPHIGTDKLPKVVKNIREYIEELGGEIRFNTRVTDILIEDGRVKGVVTNDGEEIE 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 259 CDHVVLAVGHSARDTFQMLHDRGVYIEAKPFSLGFRIEHPQGVIDRSRFGKFAGHKQLGAADYKVVHHCSN-GRAVYSFC 337
Cdd:COG2509  189 ADAVILAPGHSARDWFEMLHRLGVKLEAKPFDIGVRVEHPQELIDRIQYGKFAGHPLLGAAEYKLVYQTKNyGRGVYTFC 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 338 MCPGGTVVAATSEPGRVVTNGMSQYSRAERNANAGIVVGITPDDYPGGPLAGIAFQRKWEERAFELGGGNYMAPGQLVGD 417
Cdd:COG2509  269 MCPGGFVVAEASEPGLVVVNGMSYSDRKSENANFALLVSVTPTDFPGGPLAGIEYQRSIERLANELGGGNYKAPAQRLGD 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 418 FIAGRPSTSLGSVVPSYKPGVHPTDLSTALPDYVIEAIREALPQLEKKIAGFAMHDAVLTGVETRTSSPIRVRRRDDYQS 497
Cdd:COG2509  349 FLAGRRSTELGSVEPTYKPGVTPGDLSLVLPYRILDALREALEAFDKKIPGFASDDALLYGVETRTSSPVRIPRDEDLET 428

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 504816830 498 mNVEGLYPagegagyaggIYSAAIDGIEVAEAVALKMTG 536
Cdd:COG2509  429 -NIKGLYPagegagyaggIVSAAVDGIRVAEAIAEKLGP 466
PRK07233 PRK07233
hypothetical protein; Provisional
 104-266 1.23e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 54.12  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILER-----GKAVRERTKD----------------TFGLWRKsvLNPESNVQFGEG 162
Cdd:PRK07233   3 AIVGGGIAGLAAAYRLAKRGHEVTVFEAddqlgGLAASFEFGGlpierfyhhifksdeaLLELLDE--LGLEDKLRWRET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 163 GAGTFSDGKLYS-----------------------------QIKDPK-------------HYGRKVLDEFVR-------A 193
Cdd:PRK07233  81 KTGYYVDGKLYPlgtplellrfphlslidkfrlglltllarRIKDWRaldkvpaeewlrrWSGEGVYEVFWEplleskfG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 194 GAPEDILY---LSRPHIGTFRLVS---------------MVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLStGE 255
Cdd:PRK07233 161 DYADDVSAawlWSRIKRRGNRRYSlfgeklgyleggfatLIDALAEAIEARGGEIRLGTPVTSVVIDGGGVTGVEVD-GE 239

                        250
                 ....*....|.
gi 504816830 256 TLRCDHVVLAV 266
Cdd:PRK07233 240 EEDFDAVISTA 250
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 104-270 9.52e-06

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: 47.71  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  104 VVIGMGPCGLFAGLILAQMGFRPIILERgkavRERTKDTFglwRKSVLNPESNVQFGEGGagtfsdgklysqikdpkhyg 183
Cdd:pfam01494   5 LIVGGGPAGLMLALLLARAGVRVVLVER----HATTSVLP---RAHGLNQRTMELLRQAG-------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  184 rkVLDEFVRAGAPEDI----LYLSRPHIGTFRLVS----------MVEK-MRATIHELGGEVRFQTRVDDIEIDQGKV-- 246
Cdd:pfam01494  58 --LEDRILAEGVPHEGmglaFYNTRRRADLDFLTSpprvtvypqtELEPiLVEHAEARGAQVRFGTEVLSLEQDGDGVta 135

                         170       180
                  ....*....|....*....|....*..
gi 504816830  247 --RGLKLSTGETLRCDHVVLAVG-HSA 270
Cdd:pfam01494 136 vvRDRRDGEEYTVRAKYLVGCDGgRSP 162
 
Name Accession Description Interval E-value
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
99-536 0e+00

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 752.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  99 TAPRPVVIGMGPCGLFAGLILAQMGFRPIILERGKAVRERTKDTFGLWRKSVLNPESNVQFGEGGAGTFSDGKLYSQIKD 178
Cdd:COG2509   29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDVEERTCPVAEFWRKGKCNPESNIQFGEGGAGTFSDGKLNTRSKD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 179 PKHYGRKVLDEFVRAGAPEDILYLSRPHIGTFRLVSMVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTGETLR 258
Cdd:COG2509  109 PQGLIRYVLEIFVKFGAPEEILYAAKPHIGTDKLPKVVKNIREYIEELGGEIRFNTRVTDILIEDGRVKGVVTNDGEEIE 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 259 CDHVVLAVGHSARDTFQMLHDRGVYIEAKPFSLGFRIEHPQGVIDRSRFGKFAGHKQLGAADYKVVHHCSN-GRAVYSFC 337
Cdd:COG2509  189 ADAVILAPGHSARDWFEMLHRLGVKLEAKPFDIGVRVEHPQELIDRIQYGKFAGHPLLGAAEYKLVYQTKNyGRGVYTFC 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 338 MCPGGTVVAATSEPGRVVTNGMSQYSRAERNANAGIVVGITPDDYPGGPLAGIAFQRKWEERAFELGGGNYMAPGQLVGD 417
Cdd:COG2509  269 MCPGGFVVAEASEPGLVVVNGMSYSDRKSENANFALLVSVTPTDFPGGPLAGIEYQRSIERLANELGGGNYKAPAQRLGD 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 418 FIAGRPSTSLGSVVPSYKPGVHPTDLSTALPDYVIEAIREALPQLEKKIAGFAMHDAVLTGVETRTSSPIRVRRRDDYQS 497
Cdd:COG2509  349 FLAGRRSTELGSVEPTYKPGVTPGDLSLVLPYRILDALREALEAFDKKIPGFASDDALLYGVETRTSSPVRIPRDEDLET 428

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 504816830 498 mNVEGLYPagegagyaggIYSAAIDGIEVAEAVALKMTG 536
Cdd:COG2509  429 -NIKGLYPagegagyaggIVSAAVDGIRVAEAIAEKLGP 466
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 214-277 2.79e-10

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 62.56  E-value: 2.79e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504816830 214 SMVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTGETLRCDHVVLAVghSARDTFQML 277
Cdd:COG1233  223 ALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRADAVVSNA--DPAHTYLRL 284
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 220-270 3.09e-09

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: 59.10  E-value: 3.09e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504816830 220 RATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTGETLRCDHVVLAVGHSA 270
Cdd:COG3349  219 LAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADGETVPADAVVLAVPPEV 269
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
109-271 6.42e-08

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 54.20  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 109 GPCGLFAGLILAQMGFRPIILERGKAVRE---------RTKDTFGLWRKS--VLNPESNVQFgeggagTFSDGKlYSQIK 177
Cdd:COG0644    2 GPAGSAAARRLARAGLSVLLLEKGSFPGDkicgggllpRALEELEPLGLDepLERPVRGARF------YSPGGK-SVELP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 178 DPKHYG----RKVLDEFVRAGApedilylsrphigtfrlvsmvekmratiHELGGEVRFQTRVDDIEIDQGKVRgLKLST 253
Cdd:COG0644   75 PGRGGGyvvdRARFDRWLAEQA----------------------------EEAGAEVRTGTRVTDVLRDDGRVV-VRTGD 125

                        170
                 ....*....|....*...
gi 504816830 254 GETLRCDHVVLAVGHSAR 271
Cdd:COG0644  126 GEEIRADYVVDADGARSL 143
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
104-280 7.52e-08

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 54.53  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILERGKAVRERTKDTFGLWRKSVLNP--ESNVQFGEGGAGTFSD------------ 169
Cdd:COG0665    6 VVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGASGRNAGQLRPGLAALadRALVRLAREALDLWRElaaelgidcdfr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 170 --GKLY------------SQIKDPKHYGRKVldEFV-RAGAPEDILYLSRPHI---------GTFRLVSMVEKMRATIHE 225
Cdd:COG0665   86 rtGVLYlarteaelaalrAEAEALRALGLPV--ELLdAAELREREPGLGSPDYagglydpddGHVDPAKLVRALARAARA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504816830 226 LGGEVRFQTRVDDIEIDQGKVRGLKLSTGeTLRCDHVVLAVGHSARDTFQMLHDR 280
Cdd:COG0665  164 AGVRIREGTPVTGLEREGGRVTGVRTERG-TVRADAVVLAAGAWSARLLPMLGLR 217
PRK07233 PRK07233
hypothetical protein; Provisional
 104-266 1.23e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 54.12  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILER-----GKAVRERTKD----------------TFGLWRKsvLNPESNVQFGEG 162
Cdd:PRK07233   3 AIVGGGIAGLAAAYRLAKRGHEVTVFEAddqlgGLAASFEFGGlpierfyhhifksdeaLLELLDE--LGLEDKLRWRET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 163 GAGTFSDGKLYS-----------------------------QIKDPK-------------HYGRKVLDEFVR-------A 193
Cdd:PRK07233  81 KTGYYVDGKLYPlgtplellrfphlslidkfrlglltllarRIKDWRaldkvpaeewlrrWSGEGVYEVFWEplleskfG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 194 GAPEDILY---LSRPHIGTFRLVS---------------MVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLStGE 255
Cdd:PRK07233 161 DYADDVSAawlWSRIKRRGNRRYSlfgeklgyleggfatLIDALAEAIEARGGEIRLGTPVTSVVIDGGGVTGVEVD-GE 239

                        250
                 ....*....|.
gi 504816830 256 TLRCDHVVLAV 266
Cdd:PRK07233 240 EEDFDAVISTA 250
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 104-265 6.49e-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: 51.48  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILERGKAVRERTK------------DTFGLWRksvlnpesnvQFGEGGA----GTF 167
Cdd:COG0654    7 LIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRgialsprslellRRLGLWD----------RLLARGApirgIRV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 168 SDGklysqikdpkHYGRKVLDEFVRAGAPEDILYLSRPHIGTFrlvsmvekMRATIHELGGEVRFQTRVDDIEIDQGKVR 247
Cdd:COG0654   77 RDG----------SDGRVLARFDAAETGLPAGLVVPRADLERA--------LLEAARALGVELRFGTEVTGLEQDADGVT 138

                        170
                 ....*....|....*...
gi 504816830 248 gLKLSTGETLRCDHVVLA 265
Cdd:COG0654  139 -VTLADGRTLRADLVVGA 155
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 204-270 5.13e-06

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: 49.06  E-value: 5.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504816830 204 RPHIGTFR--LVSMVEKMRATIHElgGEVRFQTRVDDIEIDQGKVRgLKLSTGETLRCDHVVLAVGHSA 270
Cdd:COG1232  199 GEVFGYLRggLGTLVEALAEALEA--GEIRLGTRVTAIEREGGGWR-VTTSDGETIEADAVVSATPAPA 264
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 104-270 9.52e-06

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: 47.71  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  104 VVIGMGPCGLFAGLILAQMGFRPIILERgkavRERTKDTFglwRKSVLNPESNVQFGEGGagtfsdgklysqikdpkhyg 183
Cdd:pfam01494   5 LIVGGGPAGLMLALLLARAGVRVVLVER----HATTSVLP---RAHGLNQRTMELLRQAG-------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830  184 rkVLDEFVRAGAPEDI----LYLSRPHIGTFRLVS----------MVEK-MRATIHELGGEVRFQTRVDDIEIDQGKV-- 246
Cdd:pfam01494  58 --LEDRILAEGVPHEGmglaFYNTRRRADLDFLTSpprvtvypqtELEPiLVEHAEARGAQVRFGTEVLSLEQDGDGVta 135

                         170       180
                  ....*....|....*....|....*..
gi 504816830  247 --RGLKLSTGETLRCDHVVLAVG-HSA 270
Cdd:pfam01494 136 vvRDRRDGEEYTVRAKYLVGCDGgRSP 162
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 104-268 2.74e-05

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: 46.39  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILERGKAVrertkdtFGLWRksvLN--PesnvqfgegGAGTFSDGKLYS-----QI 176
Cdd:COG2072   10 VVIGAGQAGLAAAYHLRRAGIDFVVLEKADDV-------GGTWR---DNryP---------GLRLDTPSHLYSlpffpNW 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 177 KDPKHYgrkvldefvrAGAPEdIL-YLSRphigtfrlvsMVEKmratiHELGGEVRFQTRVDDIEIDQGkvRG---LKLS 252
Cdd:COG2072   71 SDDPDF----------PTGDE-ILaYLEA----------YADK-----FGLRRPIRFGTEVTSARWDEA--DGrwtVTTD 122

                        170
                 ....*....|....*.
gi 504816830 253 TGETLRCDHVVLAVGH 268
Cdd:COG2072  123 DGETLTARFVVVATGP 138
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
201-274 4.69e-05

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


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 46.10  E-value: 4.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504816830 201 YLSRPHIGTFrLVSMVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRgLKLSTGETLRCDHVVLAVGHSARDTF 274
Cdd:COG4529   95 FVPRRLFGEY-LRERLAEALARAPAGVRLRHIRAEVVDLERDDGGYR-VTLADGETLRADAVVLATGHPPPAPP 166
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 214-275 3.43e-04

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 43.25  E-value: 3.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504816830  214 SMVEKMRATIheLGGEVRFQTRVDDIEIDQGKVRgLKLSTGETLRCDHVVLAV--GHSARDTFQ 275
Cdd:pfam01593 207 ALPDALAAQL--LGGDVRLNTRVRSIDREGDGVT-VTLTDGEVIEADAVIVTVplGVLKRILFT 267
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
215-267 8.70e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 41.78  E-value: 8.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504816830 215 MVEKMRATIHELGGEVRFQTRVDDIEIDQGKVRGLKLSTG----ETLRCDHVVLAVG 267
Cdd:PRK08274 133 LVNALYRSAERLGVEIRYDAPVTALELDDGRFVGARAGSAaggaERIRAKAVVLAAG 189
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
92-131 8.72e-04

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 41.82  E-value: 8.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504816830  92 AKAPAQLTAPrPVVIGMGPCGLFAGLILAQMGFRPIILER 131
Cdd:PRK06183   3 AQHPDAHDTD-VVIVGAGPVGLTLANLLGQYGVRVLVLER 41
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
104-271 9.62e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 41.26  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 104 VVIGMGPCGLFAGLILAQMGFRPIILERGKAvrertkdtfglwrksvlnpesnvqfgeGGAGTfsdgkLYSQIKDPkhyg 183
Cdd:COG0492    4 VIIGAGPAGLTAAIYAARAGLKTLVIEGGEP---------------------------GGQLA-----TTKEIENY---- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816830 184 rkvldefvrAGAPEDILylsrphiGTfrlvSMVEKMRATIHELGGEVRFqTRVDDIEIDQGKVRgLKLSTGETLRCDHVV 263
Cdd:COG0492   48 ---------PGFPEGIS-------GP----ELAERLREQAERFGAEILL-EEVTSVDKDDGPFR-VTTDDGTEYEAKAVI 105


                 ....*...
gi 504816830 264 LAVGHSAR 271
Cdd:COG0492  106 IATGAGPR 113
PLN02612 PLN02612
phytoene desaturase
 223-266 7.88e-03

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 39.06  E-value: 7.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 504816830 223 IHELGGEVRFQTRVDDIEI-DQGKVRGLKLSTGETLRCDHVVLAV 266
Cdd:PLN02612 318 FQSLGGEVRLNSRIKKIELnDDGTVKHFLLTNGSVVEGDVYVSAT 362
 
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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