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Conserved domains on  [gi|15597541|ref|NP_251035|]
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hypothetical protein PA2345 [Pseudomonas aeruginosa PAO1]

Protein Classification

FAD/NAD(P)-binding oxidoreductase( domain architecture ID 11418561)

FAD/NAD(P)-binding oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to sulfide:quinone oxidoreductase which catalyzes the oxidation of hydrogen sulfide using quinone as the electron acceptor

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
31-358 3.98e-59

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: 195.42  E-value: 3.98e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541  31 KRSPGLRISLIEPADTHYYQP--GWTLVGGGAYAQGDT-ARPMAGLVPPGVEW-LRTRVERVDPEARRLLLEGGDSLEYR 106
Cdd:COG0446   1 RLGPDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPEDLlVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 107 NLIVCPGLRLAWERIEGLEEtlgrNGVTSNYRYDLAPYTWELVRGLRGGKALFTQPAmPIkcagapqkaMYLSCDHWLRE 186
Cdd:COG0446  81 KLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVIGGG-PI---------GLELAEALRKR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 187 GvlqdIEVEFDLAGAALFGVAD--FVPPLMEYVRKYSAELAFNSNLVKVDGAARKAwfeVKDADGNtnlaEKDFDLLHVV 264
Cdd:COG0446 147 G----LKVTLVERAPRLLGVLDpeMAALLEEELREHGVELRLGETVVAIDGDDKVA---VTLTDGE----EIPADLVVVA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 265 PPQLPPTFVA-ASGLG-DAAGWCEVDPaTLQHvRHGEIFALGDVCGTANAKTAAAAR--------KQIVVVAENLLglrs 334
Cdd:COG0446 216 PGVRPNTELAkDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPHPVTGKTVYiplasaanKQGRVAAENIL---- 289
                       330       340       350
                ....*....|....*....|....*....|..
gi 15597541 335 grGLPLRYDG--------YGGCPLTVERGRVV 358
Cdd:COG0446 290 --GGPAPFPGlgtfiskvFDLCIASTGTGRLL 319
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
31-358 3.98e-59

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: 195.42  E-value: 3.98e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541  31 KRSPGLRISLIEPADTHYYQP--GWTLVGGGAYAQGDT-ARPMAGLVPPGVEW-LRTRVERVDPEARRLLLEGGDSLEYR 106
Cdd:COG0446   1 RLGPDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPEDLlVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 107 NLIVCPGLRLAWERIEGLEEtlgrNGVTSNYRYDLAPYTWELVRGLRGGKALFTQPAmPIkcagapqkaMYLSCDHWLRE 186
Cdd:COG0446  81 KLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVIGGG-PI---------GLELAEALRKR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 187 GvlqdIEVEFDLAGAALFGVAD--FVPPLMEYVRKYSAELAFNSNLVKVDGAARKAwfeVKDADGNtnlaEKDFDLLHVV 264
Cdd:COG0446 147 G----LKVTLVERAPRLLGVLDpeMAALLEEELREHGVELRLGETVVAIDGDDKVA---VTLTDGE----EIPADLVVVA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 265 PPQLPPTFVA-ASGLG-DAAGWCEVDPaTLQHvRHGEIFALGDVCGTANAKTAAAAR--------KQIVVVAENLLglrs 334
Cdd:COG0446 216 PGVRPNTELAkDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPHPVTGKTVYiplasaanKQGRVAAENIL---- 289
                       330       340       350
                ....*....|....*....|....*....|..
gi 15597541 335 grGLPLRYDG--------YGGCPLTVERGRVV 358
Cdd:COG0446 290 --GGPAPFPGlgtfiskvFDLCIASTGTGRLL 319
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
31-358 3.98e-59

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: 195.42  E-value: 3.98e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541  31 KRSPGLRISLIEPADTHYYQP--GWTLVGGGAYAQGDT-ARPMAGLVPPGVEW-LRTRVERVDPEARRLLLEGGDSLEYR 106
Cdd:COG0446   1 RLGPDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPEDLlVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 107 NLIVCPGLRLAWERIEGLEEtlgrNGVTSNYRYDLAPYTWELVRGLRGGKALFTQPAmPIkcagapqkaMYLSCDHWLRE 186
Cdd:COG0446  81 KLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVIGGG-PI---------GLELAEALRKR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 187 GvlqdIEVEFDLAGAALFGVAD--FVPPLMEYVRKYSAELAFNSNLVKVDGAARKAwfeVKDADGNtnlaEKDFDLLHVV 264
Cdd:COG0446 147 G----LKVTLVERAPRLLGVLDpeMAALLEEELREHGVELRLGETVVAIDGDDKVA---VTLTDGE----EIPADLVVVA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 265 PPQLPPTFVA-ASGLG-DAAGWCEVDPaTLQHvRHGEIFALGDVCGTANAKTAAAAR--------KQIVVVAENLLglrs 334
Cdd:COG0446 216 PGVRPNTELAkDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPHPVTGKTVYiplasaanKQGRVAAENIL---- 289
                       330       340       350
                ....*....|....*....|....*....|..
gi 15597541 335 grGLPLRYDG--------YGGCPLTVERGRVV 358
Cdd:COG0446 290 --GGPAPFPGlgtfiskvFDLCIASTGTGRLL 319
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
31-406 9.06e-28

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 112.92  E-value: 9.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541  31 KRSPGLRISLIEPADTHYYQPGWTLVGGGAYAQGDTARPMAGLVPP-GVEWLRTRVERVDPEARRLLLEGGDSLEYRNLI 109
Cdd:COG1252  23 KLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRaGVRFIQGEVTGIDPEARTVTLADGRTLSYDYLV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 110 VCPGLRLAWERIEGLEEtlgrNGVtSNYRYDLAPYTWELVRGLRggKALFTQPAMPIKCAGAPQKA--MYLSCDHWLRE- 186
Cdd:COG1252 103 IATGSVTNFFGIPGLAE----HAL-PLKTLEDALALRERLLAAF--ERAERRRLLTIVVVGGGPTGveLAGELAELLRKl 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 187 ----GVLQDiEVEFDL--AGAALFGvaDFVPPLMEYVRKYSAELA----FNSNLVKVDGAArkawfeVKDADGNtnlaEK 256
Cdd:COG1252 176 lrypGIDPD-KVRITLveAGPRILP--GLGEKLSEAAEKELEKRGvevhTGTRVTEVDADG------VTLEDGE----EI 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597541 257 DFDLLHVVPPQLPPTFVAASGL-GDAAGWCEVDPaTLQHVRHGEIFALGDVCGTANAKTAAAAR------KQIVVVAENL 329
Cdd:COG1252 243 PADTVIWAAGVKAPPLLADLGLpTDRRGRVLVDP-TLQVPGHPNVFAIGDCAAVPDPDGKPVPKtaqaavQQAKVLAKNI 321
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597541 330 LGLRSGRGL-PLRYDGYgGCPLTVERGRVVLAefgyagklLPTFPLEptaaSRFAWLLKRhvlpWVYWNAMLKGREWL 406
Cdd:COG1252 322 AALLRGKPLkPFRYRDK-GCLASLGRGAAVAD--------VGGLKLS----GFLAWLLKR----AIHLYFLPGFRGRL 382
 
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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