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Conserved domains on  [gi|2126438373|ref|WP_227502956|]
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FAD/NAD(P)-binding oxidoreductase [Acinetobacter baumannii]

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

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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 ...
12-335 2.56e-56

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: 187.33  E-value: 2.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  12 PHLDIVIIDPADSHYYQP--GWTMVGGGIFKP-QITARSMASVIPSKVKW-MKAAVAGFDPEHNQIILEGCQPIQYKALV 87
Cdd:COG0446     4 PDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPeDLLVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYDKLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  88 VCPGLKLNWHGIEGlvetLGKNGVTSNYRYDLAPYTWELVQQLNSGTAIFTQppmpikcaGAPqkAMYLSADYWLKQGkl 167
Cdd:COG0446    84 LATGARPRPPPIPG----LDLPGVFTLRTLDDADALREALKEFKGKRAVVIG--------GGP--IGLELAEALRKRG-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 168 KDISIHFYNSGgvLFGV--KEYVPALMQYVEKYGTELHFNHQLAKVDGPAK-KAWFKvvNDEnaalvETDFDMLHVVPPq 244
Cdd:COG0446   148 LKVTLVERAPR--LLGVldPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLT--DGE-----EIPADLVVVAPG- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 245 QAPDF--IRASTL-TDDAGWVSVNPqTLQhTQHANIFALGDVMNAPNAKTAAAARAQA--------PIVAVNVIaqlkGE 313
Cdd:COG0446   218 VRPNTelAKDAGLaLGERGWIKVDE-TLQ-TSDPDVYAAGDCAEVPHPVTGKTVYIPLasaankqgRVAAENIL----GG 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 2126438373 314 PnfCEYNG--------YGSCPLTVERGKIV 335
Cdd:COG0446   292 P--APFPGlgtfiskvFDLCIASTGTGRLL 319
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
12-335 2.56e-56

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: 187.33  E-value: 2.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  12 PHLDIVIIDPADSHYYQP--GWTMVGGGIFKP-QITARSMASVIPSKVKW-MKAAVAGFDPEHNQIILEGCQPIQYKALV 87
Cdd:COG0446     4 PDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPeDLLVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYDKLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  88 VCPGLKLNWHGIEGlvetLGKNGVTSNYRYDLAPYTWELVQQLNSGTAIFTQppmpikcaGAPqkAMYLSADYWLKQGkl 167
Cdd:COG0446    84 LATGARPRPPPIPG----LDLPGVFTLRTLDDADALREALKEFKGKRAVVIG--------GGP--IGLELAEALRKRG-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 168 KDISIHFYNSGgvLFGV--KEYVPALMQYVEKYGTELHFNHQLAKVDGPAK-KAWFKvvNDEnaalvETDFDMLHVVPPq 244
Cdd:COG0446   148 LKVTLVERAPR--LLGVldPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLT--DGE-----EIPADLVVVAPG- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 245 QAPDF--IRASTL-TDDAGWVSVNPqTLQhTQHANIFALGDVMNAPNAKTAAAARAQA--------PIVAVNVIaqlkGE 313
Cdd:COG0446   218 VRPNTelAKDAGLaLGERGWIKVDE-TLQ-TSDPDVYAAGDCAEVPHPVTGKTVYIPLasaankqgRVAAENIL----GG 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 2126438373 314 PnfCEYNG--------YGSCPLTVERGKIV 335
Cdd:COG0446   292 P--APFPGlgtfiskvFDLCIASTGTGRLL 319
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
173-283 4.32e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.01  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 173 HFYNSGGV---LFGVKEYV-----PALMQYVEKY-GTE--LHFNHQLAKVDGPAKKawFKVVNDENAALVETDFDMLHV- 240
Cdd:PRK06292  186 QALSRLGVkvtVFERGDRIlpledPEVSKQAQKIlSKEfkIKLGAKVTSVEKSGDE--KVEELEKGGKTETIEADYVLVa 263
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2126438373 241 ---VPPQQAPDFIRASTLTDDAGWVSVNPQTLqhTQHANIFALGDV 283
Cdd:PRK06292  264 tgrRPNTDGLGLENTGIELDERGRPVVDEHTQ--TSVPGIYAAGDV 307
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
12-335 2.56e-56

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: 187.33  E-value: 2.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  12 PHLDIVIIDPADSHYYQP--GWTMVGGGIFKP-QITARSMASVIPSKVKW-MKAAVAGFDPEHNQIILEGCQPIQYKALV 87
Cdd:COG0446     4 PDAEITVIEKGPHHSYQPcgLPYYVGGGIKDPeDLLVRTPESFERKGIDVrTGTEVTAIDPEAKTVTLRDGETLSYDKLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  88 VCPGLKLNWHGIEGlvetLGKNGVTSNYRYDLAPYTWELVQQLNSGTAIFTQppmpikcaGAPqkAMYLSADYWLKQGkl 167
Cdd:COG0446    84 LATGARPRPPPIPG----LDLPGVFTLRTLDDADALREALKEFKGKRAVVIG--------GGP--IGLELAEALRKRG-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 168 KDISIHFYNSGgvLFGV--KEYVPALMQYVEKYGTELHFNHQLAKVDGPAK-KAWFKvvNDEnaalvETDFDMLHVVPPq 244
Cdd:COG0446   148 LKVTLVERAPR--LLGVldPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLT--DGE-----EIPADLVVVAPG- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 245 QAPDF--IRASTL-TDDAGWVSVNPqTLQhTQHANIFALGDVMNAPNAKTAAAARAQA--------PIVAVNVIaqlkGE 313
Cdd:COG0446   218 VRPNTelAKDAGLaLGERGWIKVDE-TLQ-TSDPDVYAAGDCAEVPHPVTGKTVYIPLasaankqgRVAAENIL----GG 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 2126438373 314 PnfCEYNG--------YGSCPLTVERGKIV 335
Cdd:COG0446   292 P--APFPGlgtfiskvFDLCIASTGTGRLL 319
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
12-383 2.12e-31

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 122.93  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  12 PHLDIVIIDPADSHYYQPGWTMVGGGIFKPQITARSMASVI-PSKVKWMKAAVAGFDPEHNQIILEGCQPIQYKALVVCP 90
Cdd:COG1252    26 GDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLrRAGVRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIAT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373  91 GLKLNWHGIEGLVEtlgkNGVtSNYRYDLAPYTWELVQQL-------NSGT-AIFTQPPMPIKCAGapqkAMYLSADYWL 162
Cdd:COG1252   106 GSVTNFFGIPGLAE----HAL-PLKTLEDALALRERLLAAferaerrRLLTiVVVGGGPTGVELAG----ELAELLRKLL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 163 KQGKL--KDISIHFYNSGGVLFGV--KEYVPALMQYVEKYGTELHFNHQLAKVDgpAKKAWFKvvNDEnaalvETDFDML 238
Cdd:COG1252   177 RYPGIdpDKVRITLVEAGPRILPGlgEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADGVTLE--DGE-----EIPADTV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 239 HVVPPQQAPDFIRASTL-TDDAGWVSVNPqTLQHTQHANIFALGDVMNapnakTAAAARAQAPIVAV-----------NV 306
Cdd:COG1252   248 IWAAGVKAPPLLADLGLpTDRRGRVLVDP-TLQVPGHPNVFAIGDCAA-----VPDPDGKPVPKTAQaavqqakvlakNI 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2126438373 307 IAQLKGEP--NFcEYNGYGsCPLTVERGKIVLaefgyggkllpSFPKWVIDGqkpsRLAWLLKEQILppIYWQGMLKGR 383
Cdd:COG1252   322 AALLRGKPlkPF-RYRDKG-CLASLGRGAAVA-----------DVGGLKLSG----FLAWLLKRAIH--LYFLPGFRGR 381
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
173-283 4.32e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.01  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 173 HFYNSGGV---LFGVKEYV-----PALMQYVEKY-GTE--LHFNHQLAKVDGPAKKawFKVVNDENAALVETDFDMLHV- 240
Cdd:PRK06292  186 QALSRLGVkvtVFERGDRIlpledPEVSKQAQKIlSKEfkIKLGAKVTSVEKSGDE--KVEELEKGGKTETIEADYVLVa 263
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2126438373 241 ---VPPQQAPDFIRASTLTDDAGWVSVNPQTLqhTQHANIFALGDV 283
Cdd:PRK06292  264 tgrRPNTDGLGLENTGIELDERGRPVVDEHTQ--TSVPGIYAAGDV 307
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
190-284 5.51e-03

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 38.61  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126438373 190 ALMQYVEKYGTELHFNHQLAKVDGPAkkAWFKVVNDENaalvetdFDM-LHVVPPQQAPDFIRASTLT-DDAGWVSVNPQ 267
Cdd:PRK13512  194 PILDELDKREIPYRLNEEIDAINGNE--VTFKSGKVEH-------YDMiIEGVGTHPNSKFIESSNIKlDDKGFIPVNDK 264
                          90
                  ....*....|....*..
gi 2126438373 268 TlqHTQHANIFALGDVM 284
Cdd:PRK13512  265 F--ETNVPNIYAIGDII 279
 
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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