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Conserved domains on  [gi|1131021033|ref|WP_075780622|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified Marinitoga]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11422994)

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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0050660|GO:0016491
PubMed:  33684359

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-316 1.01e-44

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 156.82  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   5 TDVVIIGggaagmaaayS----------ATREGADVILLERDEdTGGVLNQ--CIHNGFGlhyFKKDLTGPEFKELAKER 72
Cdd:COG0492     1 YDVVIIG----------AgpagltaaiyAARAGLKTLVIEGGE-PGGQLATtkEIENYPG---FPEGISGPELAERLREQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  73 IKDLN--ILYGTyVLEVTKDKRIIFVDRRGIHEIETKALVMATGARERHfnsLPVPGKR---ITGVFTAGLAQRFinlen 147
Cdd:COG0492    67 AERFGaeILLEE-VTSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRK---LGLPGEEefeGRGVSYCATCDGF----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 148 LKPGNKAVILGSGDIGLIMARRLTLEGIKVEAVL---EIMPypgglERNIQQCLRDF-NIPLYLSHTVTAIEGEKRLEKV 223
Cdd:COG0492   138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHrrdELRA-----SKILVERLRANpKIEVLWNTEVTEIEGDGRVEGV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 224 IASQVDykwnpiPGTEKVFDVDMLITSVGLIPSTKPVD--FVDADP-GF-LVSNTNQTSEDWIFAAGNCT-VIFDLVDFV 298
Cdd:COG0492   213 TLKNVK------TGEEKELEVDGVFVAIGLKPNTELLKglGLELDEdGYiVVDEDMETSVPGVFAAGDVRdYKYRQAATA 286
                         330
                  ....*....|....*...
gi 1131021033 299 AKEGEKAGKYAALYAQGK 316
Cdd:COG0492   287 AGEGAIAALSAARYLEPL 304
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-316 1.01e-44

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 156.82  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   5 TDVVIIGggaagmaaayS----------ATREGADVILLERDEdTGGVLNQ--CIHNGFGlhyFKKDLTGPEFKELAKER 72
Cdd:COG0492     1 YDVVIIG----------AgpagltaaiyAARAGLKTLVIEGGE-PGGQLATtkEIENYPG---FPEGISGPELAERLREQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  73 IKDLN--ILYGTyVLEVTKDKRIIFVDRRGIHEIETKALVMATGARERHfnsLPVPGKR---ITGVFTAGLAQRFinlen 147
Cdd:COG0492    67 AERFGaeILLEE-VTSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRK---LGLPGEEefeGRGVSYCATCDGF----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 148 LKPGNKAVILGSGDIGLIMARRLTLEGIKVEAVL---EIMPypgglERNIQQCLRDF-NIPLYLSHTVTAIEGEKRLEKV 223
Cdd:COG0492   138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHrrdELRA-----SKILVERLRANpKIEVLWNTEVTEIEGDGRVEGV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 224 IASQVDykwnpiPGTEKVFDVDMLITSVGLIPSTKPVD--FVDADP-GF-LVSNTNQTSEDWIFAAGNCT-VIFDLVDFV 298
Cdd:COG0492   213 TLKNVK------TGEEKELEVDGVFVAIGLKPNTELLKglGLELDEdGYiVVDEDMETSVPGVFAAGDVRdYKYRQAATA 286
                         330
                  ....*....|....*...
gi 1131021033 299 AKEGEKAGKYAALYAQGK 316
Cdd:COG0492   287 AGEGAIAALSAARYLEPL 304
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-290 9.36e-20

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: 88.91  E-value: 9.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   5 TDVVIIGGGAAGMAAAYSATREGADVILLErdEDTGGVLNQCIHNGFGLHY---FKKDLTGPEFKELAKERIKDLN---- 77
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE--DEGTCPYGGCVLSKALLGAaeaPEIASLWADLYKRKEEVVKKLNngie 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  78 ILYGTYVLEVTKDKRIIFV---DRRGIHEIETKALVMATGARERHfnsLPVPG---KRITGVFTAGLAQRfINLENLkpG 151
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLeelVDGDGETITYDRLVIATGARPRL---PPIPGvelNVGFLVRTLDSAEA-LRLKLL--P 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 152 NKAVILGSGDIGL---IMARRLTLEGIKVEAVLEIMP-YPGGLERNIQQCLRDFNIPLYLSHTVTAIEGEKRLEKVIAsq 227
Cdd:pfam07992 153 KRVVVVGGGYIGVelaAALAKLGKEVTLIEALDRLLRaFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL-- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131021033 228 vdykwnpipGTEKVFDVDMLITSVGLIPSTKPVDF----VDADPGFLVSNTNQTSEDWIFAAGNCTV 290
Cdd:pfam07992 231 ---------KDGTEIDADLVVVAIGRRPNTELLEAagleLDERGGIVVDEYLRTSVPGIYAAGDCRV 288
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
54-316 1.46e-08

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 56.76  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  54 HYFKKDLTGPEFKELAKERIKdlnILYGTYVLEVTKDKRIIFVDRRGIHEIETkaLVMATGARErhfNSLPVPGKRITGV 133
Cdd:TIGR02374  50 EADLDDITLNSKDWYEKHGIT---LYTGETVIQIDTDQKQVITDAGRTLSYDK--LILATGSYP---FILPIPGADKKGV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 134 FT----------AGLAQRFinlenlkpgNKAVILGSGDIGLIMARRLTLEGIKVeAVLEIMPY--------PGGleRNIQ 195
Cdd:TIGR02374 122 YVfrtiedldaiMAMAQRF---------KKAAVIGGGLLGLEAAVGLQNLGMDV-SVIHHAPGlmakqldqTAG--RLLQ 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 196 QCLRDFNIPLYLSHTVTAIEGEKRLEKVIASQvdykwnpipGTEkvFDVDMLITSVGLIPSTK--PVDFVDADPGFLVSN 273
Cdd:TIGR02374 190 RELEQKGLTFLLEKDTVEIVGATKADRIRFKD---------GSS--LEADLIVMAAGIRPNDElaVSAGIKVNRGIIVND 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1131021033 274 TNQTSEDWIFAAGNCTvifdlvdfvAKEGEKAGKYAALYAQGK 316
Cdd:TIGR02374 259 SMQTSDPDIYAVGECA---------EHNGRVYGLVAPLYEQAK 292
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
7-295 2.34e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 55.82  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   7 VVIIGGGAAGMAAAYSATR--EGADVILLERDEDTGgvLNQCihngfGLHYFkkdlTGPEF-----------KELAKERI 73
Cdd:PRK09564    3 IIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIVS--FGAC-----GLPYF----VGGFFddpntmiartpEEFIKSGI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  74 kDLNIlyGTYVLEVTKDKRIIFVDRRGIHEIETKA---LVMATGARERhfnSLPVPGKRITGVFTAGLAQRFINLENL-- 148
Cdd:PRK09564   72 -DVKT--EHEVVKVDAKNKTITVKNLKTGSIFNDTydkLMIATGARPI---IPPIKNINLENVYTLKSMEDGLALKELlk 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 149 KPGNK-AVILGSGDIGLIMARRLTLEGIKVEAV-LE--IMP--YPGGLERNIQQCLRDFNIPLYLSHTVTAIEGEKRLEK 222
Cdd:PRK09564  146 DEEIKnIVIIGAGFIGLEAVEAAKHLGKNVRIIqLEdrILPdsFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 223 VIASQVDYkwnpipgtekvfDVDMLITSVGLIPSTkpvDFVDADP-------GFLVSNTNQTSEDWIFAAGNCTVIFDLV 295
Cdd:PRK09564  226 VVTDKGEY------------EADVVIVATGVKPNT---EFLEDTGlktlkngAIIVDEYGETSIENIYAAGDCATIYNIV 290
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-316 1.01e-44

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 156.82  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   5 TDVVIIGggaagmaaayS----------ATREGADVILLERDEdTGGVLNQ--CIHNGFGlhyFKKDLTGPEFKELAKER 72
Cdd:COG0492     1 YDVVIIG----------AgpagltaaiyAARAGLKTLVIEGGE-PGGQLATtkEIENYPG---FPEGISGPELAERLREQ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  73 IKDLN--ILYGTyVLEVTKDKRIIFVDRRGIHEIETKALVMATGARERHfnsLPVPGKR---ITGVFTAGLAQRFinlen 147
Cdd:COG0492    67 AERFGaeILLEE-VTSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRK---LGLPGEEefeGRGVSYCATCDGF----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 148 LKPGNKAVILGSGDIGLIMARRLTLEGIKVEAVL---EIMPypgglERNIQQCLRDF-NIPLYLSHTVTAIEGEKRLEKV 223
Cdd:COG0492   138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHrrdELRA-----SKILVERLRANpKIEVLWNTEVTEIEGDGRVEGV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 224 IASQVDykwnpiPGTEKVFDVDMLITSVGLIPSTKPVD--FVDADP-GF-LVSNTNQTSEDWIFAAGNCT-VIFDLVDFV 298
Cdd:COG0492   213 TLKNVK------TGEEKELEVDGVFVAIGLKPNTELLKglGLELDEdGYiVVDEDMETSVPGVFAAGDVRdYKYRQAATA 286
                         330
                  ....*....|....*...
gi 1131021033 299 AKEGEKAGKYAALYAQGK 316
Cdd:COG0492   287 AGEGAIAALSAARYLEPL 304
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
26-295 5.11e-24

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: 101.43  E-value: 5.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  26 EGADVILLERDEDTGGVlnqcihnGFGLHYF-------KKDLTGPEFKELAKERIkdlNILYGTYVLEVTKDKRIIFVdr 98
Cdd:COG0446     4 PDAEITVIEKGPHHSYQ-------PCGLPYYvgggikdPEDLLVRTPESFERKGI---DVRTGTEVTAIDPEAKTVTL-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  99 RGIHEIETKALVMATGARERHfnsLPVPGKRITGVFTAG---LAQRFINLENLKPGNKAVILGSGDIGLIMARRLTLEGI 175
Cdd:COG0446    72 RDGETLSYDKLVLATGARPRP---PPIPGLDLPGVFTLRtldDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 176 KVEaVLEIMPYPGG-----LERNIQQCLRDFNIPLYLSHTVTAIEGEKRLEKVIASQvdykwnpipgteKVFDVDMLITS 250
Cdd:COG0446   149 KVT-LVERAPRLLGvldpeMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDG------------EEIPADLVVVA 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1131021033 251 VGLIPSTK-----PVDfVDADPGFLVSNTNQTSEDWIFAAGNCTVIFDLV 295
Cdd:COG0446   216 PGVRPNTElakdaGLA-LGERGWIKVDETLQTSDPDVYAAGDCAEVPHPV 264
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-290 9.36e-20

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: 88.91  E-value: 9.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   5 TDVVIIGGGAAGMAAAYSATREGADVILLErdEDTGGVLNQCIHNGFGLHY---FKKDLTGPEFKELAKERIKDLN---- 77
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE--DEGTCPYGGCVLSKALLGAaeaPEIASLWADLYKRKEEVVKKLNngie 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  78 ILYGTYVLEVTKDKRIIFV---DRRGIHEIETKALVMATGARERHfnsLPVPG---KRITGVFTAGLAQRfINLENLkpG 151
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLeelVDGDGETITYDRLVIATGARPRL---PPIPGvelNVGFLVRTLDSAEA-LRLKLL--P 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 152 NKAVILGSGDIGL---IMARRLTLEGIKVEAVLEIMP-YPGGLERNIQQCLRDFNIPLYLSHTVTAIEGEKRLEKVIAsq 227
Cdd:pfam07992 153 KRVVVVGGGYIGVelaAALAKLGKEVTLIEALDRLLRaFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL-- 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131021033 228 vdykwnpipGTEKVFDVDMLITSVGLIPSTKPVDF----VDADPGFLVSNTNQTSEDWIFAAGNCTV 290
Cdd:pfam07992 231 ---------KDGTEIDADLVVVAIGRRPNTELLEAagleLDERGGIVVDEYLRTSVPGIYAAGDCRV 288
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
74-316 1.85e-19

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 89.43  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  74 KDLNI--LYGTYVLEVTKDKRIIFVDRRGihEIETKALVMATGARERHfnsLPVPGKRITGVFTagL-----AQRFInlE 146
Cdd:COG1251    67 EENGIdlRLGTRVTAIDRAARTVTLADGE--TLPYDKLVLATGSRPRV---PPIPGADLPGVFT--LrtlddADALR--A 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 147 NLKPGNKAVILGSGDIGLIMARRLTLEGIKVeAVLEIMPYPggLERN--------IQQCLRDFNIPLYLSHTVTAIEGEK 218
Cdd:COG1251   138 ALAPGKRVVVIGGGLIGLEAAAALRKRGLEV-TVVERAPRL--LPRQldeeagalLQRLLEALGVEVRLGTGVTEIEGDD 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 219 RLEKVIASQvdykwnpipGTEkvFDVDMLITSVGLIPSTkpvDFVDA-----DPGFLVSNTNQTSEDWIFAAGNCTVIFD 293
Cdd:COG1251   215 RVTGVRLAD---------GEE--LPADLVVVAIGVRPNT---ELARAaglavDRGIVVDDYLRTSDPDIYAAGDCAEHPG 280
                         250       260
                  ....*....|....*....|....
gi 1131021033 294 LVDfvakeGEKAGKY-AALYAQGK 316
Cdd:COG1251   281 PVY-----GRRVLELvAPAYEQAR 299
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
95-289 2.12e-09

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: 58.94  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  95 FVDRR-----GIHEIETKALVMATGARERHFNSLPVPGKRI---TGVFtaglaqrfiNLENLkPGnKAVILGSGDIGLIM 166
Cdd:COG1249   115 FVDPHtvevtGGETLTADHIVIATGSRPRVPPIPGLDEVRVltsDEAL---------ELEEL-PK-SLVVIGGGYIGLEF 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 167 A---RRLtleGIKVEaVLEIMPYPGGLE-----RNIQQCLRDFNIPLYLSHTVTAIEGEKRLEKVIASQvdykwnpiPGT 238
Cdd:COG1249   184 AqifARL---GSEVT-LVERGDRLLPGEdpeisEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLED--------GGG 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131021033 239 EKVFDVDMLITSVGLIPSTKPVDF------VDADPGFLVSNTNQTSEDWIFAAGNCT 289
Cdd:COG1249   252 EEAVEADKVLVATGRRPNTDGLGLeaagveLDERGGIKVDEYLRTSVPGIYAIGDVT 308
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
24-291 1.24e-08

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: 56.68  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  24 TREGADVILLERDEDTGGVLnqcihngfglHYfkkdltG-PEFKeLAKERIkdlnilygtyvlevtkDKRIIFVDRRGIh 102
Cdd:COG0493   141 ARAGHEVTVFEALDKPGGLL----------RY------GiPEFR-LPKDVL----------------DREIELIEALGV- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 103 EIET-----------------KALVMATGA-RERhfnSLPVPGKRITGVFTA-----GLAQRFINLENLKPGNKAVILGS 159
Cdd:COG0493   187 EFRTnvevgkditldelleefDAVFLATGAgKPR---DLGIPGEDLKGVHSAmdfltAVNLGEAPDTILAVGKRVVVIGG 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 160 GDIG---LIMARRLTLEGIKVeavLEIMPY---PGGLERnIQQCLRDfNIPLYLSHTVTAIEGEK-------RLEKVIAS 226
Cdd:COG0493   264 GNTAmdcARTALRLGAESVTI---VYRRTReemPASKEE-VEEALEE-GVEFLFLVAPVEIIGDEngrvtglECVRMELG 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 227 QVD----YKWNPIPGTEKVFDVDMLITSVGLIPstkPVDFVDADPGFLVS---------NTNQTSEDWIFAAGNC----- 288
Cdd:COG0493   339 EPDesgrRRPVPIEGSEFTLPADLVILAIGQTP---DPSGLEEELGLELDkrgtivvdeETYQTSLPGVFAGGDAvrgps 415

                  ...
gi 1131021033 289 TVI 291
Cdd:COG0493   416 LVV 418
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
54-316 1.46e-08

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 56.76  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  54 HYFKKDLTGPEFKELAKERIKdlnILYGTYVLEVTKDKRIIFVDRRGIHEIETkaLVMATGARErhfNSLPVPGKRITGV 133
Cdd:TIGR02374  50 EADLDDITLNSKDWYEKHGIT---LYTGETVIQIDTDQKQVITDAGRTLSYDK--LILATGSYP---FILPIPGADKKGV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 134 FT----------AGLAQRFinlenlkpgNKAVILGSGDIGLIMARRLTLEGIKVeAVLEIMPY--------PGGleRNIQ 195
Cdd:TIGR02374 122 YVfrtiedldaiMAMAQRF---------KKAAVIGGGLLGLEAAVGLQNLGMDV-SVIHHAPGlmakqldqTAG--RLLQ 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 196 QCLRDFNIPLYLSHTVTAIEGEKRLEKVIASQvdykwnpipGTEkvFDVDMLITSVGLIPSTK--PVDFVDADPGFLVSN 273
Cdd:TIGR02374 190 RELEQKGLTFLLEKDTVEIVGATKADRIRFKD---------GSS--LEADLIVMAAGIRPNDElaVSAGIKVNRGIIVND 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1131021033 274 TNQTSEDWIFAAGNCTvifdlvdfvAKEGEKAGKYAALYAQGK 316
Cdd:TIGR02374 259 SMQTSDPDIYAVGECA---------EHNGRVYGLVAPLYEQAK 292
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
7-295 2.34e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 55.82  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   7 VVIIGGGAAGMAAAYSATR--EGADVILLERDEDTGgvLNQCihngfGLHYFkkdlTGPEF-----------KELAKERI 73
Cdd:PRK09564    3 IIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIVS--FGAC-----GLPYF----VGGFFddpntmiartpEEFIKSGI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  74 kDLNIlyGTYVLEVTKDKRIIFVDRRGIHEIETKA---LVMATGARERhfnSLPVPGKRITGVFTAGLAQRFINLENL-- 148
Cdd:PRK09564   72 -DVKT--EHEVVKVDAKNKTITVKNLKTGSIFNDTydkLMIATGARPI---IPPIKNINLENVYTLKSMEDGLALKELlk 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 149 KPGNK-AVILGSGDIGLIMARRLTLEGIKVEAV-LE--IMP--YPGGLERNIQQCLRDFNIPLYLSHTVTAIEGEKRLEK 222
Cdd:PRK09564  146 DEEIKnIVIIGAGFIGLEAVEAAKHLGKNVRIIqLEdrILPdsFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 223 VIASQVDYkwnpipgtekvfDVDMLITSVGLIPSTkpvDFVDADP-------GFLVSNTNQTSEDWIFAAGNCTVIFDLV 295
Cdd:PRK09564  226 VVTDKGEY------------EADVVIVATGVKPNT---EFLEDTGlktlkngAIIVDEYGETSIENIYAAGDCATIYNIV 290
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
109-287 8.21e-08

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 53.78  E-value: 8.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 109 LVMATGARERHFNSLPVPGKRITGVFTAGLAQRFinLENLKPGNKAVILGSGDIGLIMARRLTLEGIKV---EAVLEIMP 185
Cdd:PRK09754  104 LFIATGAAARPLPLLDALGERCFTLRHAGDAARL--REVLQPERSVVIVGAGTIGLELAASATQRRCKVtviELAATVMG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 186 Y--PGGLERNIQQCLRDFNIPLYL-SHTVTAIEGEKRL------EKVIASQVDYkwnpipGTEKVFDvDMLITSVGLips 256
Cdd:PRK09754  182 RnaPPPVQRYLLQRHQQAGVRILLnNAIEHVVDGEKVEltlqsgETLQADVVIY------GIGISAN-DQLAREANL--- 251
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1131021033 257 tkpvdfvDADPGFLVSNTNQTSEDWIFAAGN 287
Cdd:PRK09754  252 -------DTANGIVIDEACRTCDPAIFAGGD 275
gltD PRK12810
glutamate synthase subunit beta; Reviewed
16-288 4.66e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 48.62  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  16 GMAAAYSATREGADVILLERDEDTGGVLNqcihngFGLHYFKKDltgpefKELAKERIKDLNILYGTYVLEVTKDKRIIF 95
Cdd:PRK12810  155 GLAAADQLARAGHKVTVFERADRIGGLLR------YGIPDFKLE------KEVIDRRIELMEAEGIEFRTNVEVGKDITA 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  96 VDRRGIHEietkALVMATGARERhfNSLPVPGKRITGVFTA----GLAQRFINLENLKP-----GNKAVILGSGDIGLIM 166
Cdd:PRK12810  223 EELLAEYD----AVFLGTGAYKP--RDLGIPGRDLDGVHFAmdflIQNTRRVLGDETEPfisakGKHVVVIGGGDTGMDC 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 167 ARRLTLEGIKVEAVLEIMPYPgGLERNIQQ------------------CLRDFNIplylshTVTAIEGEK-RLEKVIASQ 227
Cdd:PRK12810  297 VGTAIRQGAKSVTQRDIMPMP-PSRRNKNNpwpywpmklevsnaheegVEREFNV------QTKEFEGENgKVTGVKVVR 369
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 228 VDYKWN---PIPGTEKVFDVDMLITSVGLIPSTKPV--DF-VDADP-GFLVSNTN--QTSEDWIFAAGNC 288
Cdd:PRK12810  370 TELGEGdfePVEGSEFVLPADLVLLAMGFTGPEAGLlaQFgVELDErGRVAAPDNayQTSNPKVFAAGDM 439
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
104-286 7.37e-06

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 47.83  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 104 IETKALVMATGARERHFNSLPVPGKRITGVFTAglaqrfINLENLkPgNKAVILGSGDIGLIMARRLTLEGIKV---EAV 180
Cdd:PRK06416  133 YTAKNIILATGSRPRELPGIEIDGRVIWTSDEA------LNLDEV-P-KSLVVIGGGYIGVEFASAYASLGAEVtivEAL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 181 LEIMPypgGLERNI-QQCLRDF---NIPLYLSHTVT-AIEGEKRLEKVIASQvdykwnpipGTEKVFDVDMLITSVGLIP 255
Cdd:PRK06416  205 PRILP---GEDKEIsKLAERALkkrGIKIKTGAKAKkVEQTDDGVTVTLEDG---------GKEETLEADYVLVAVGRRP 272
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1131021033 256 STKPVDF----VDADPGFLVSNTN-QTSEDWIFAAG 286
Cdd:PRK06416  273 NTENLGLeelgVKTDRGFIEVDEQlRTNVPNIYAIG 308
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
88-289 2.11e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 46.46  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  88 TKDKRIIFVDRRGIHEIETKALVMATGARERHFNSLPVPGKRI---TGVftaglaqrfINLENLkPGNKAVIlGSGDIGL 164
Cdd:PRK06327  128 TDAGYEIKVTGEDETVITAKHVIIATGSEPRHLPGVPFDNKIIldnTGA---------LNFTEV-PKKLAVI-GAGVIGL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 165 IMA---RRLtleGIKVeAVLEIMpyPGGLERNIQQ----CLRDFN---IPLYLSHTVTAIegekrleKVIASQVDYKWNP 234
Cdd:PRK06327  197 ELGsvwRRL---GAEV-TILEAL--PAFLAAADEQvakeAAKAFTkqgLDIHLGVKIGEI-------KTGGKGVSVAYTD 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131021033 235 IPGTEKVFDVDMLITSVGLIPSTK-----PVDFVDADPGFL-VSNTNQTSEDWIFAAGNCT 289
Cdd:PRK06327  264 ADGEAQTLEVDKLIVSIGRVPNTDglgleAVGLKLDERGFIpVDDHCRTNVPNVYAIGDVV 324
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
4-316 3.09e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 45.94  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   4 KTDVVIIGGGAAGMAAAYSATREGADVILLERDEDTGGVLNQ-CI-----------------HNGFGLHYFKKDLTGPEF 65
Cdd:PRK06292    3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVgCIpskaliaaaeafheakhAEEFGIHADGPKIDFKKV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  66 KELAKERIKDLNILYGTYVLEVTKDKRII----FVDRR----GIHEIETKALVMATGARerhfnSLPVPG------KRI- 130
Cdd:PRK06292   83 MARVRRERDRFVGGVVEGLEKKPKIDKIKgtarFVDPNtvevNGERIEAKNIVIATGSR-----VPPIPGvwlilgDRLl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 131 --TGVFtaglaqrfiNLENLkPGNKAVIlGSGDIGLIMA---RRLtleGIKVeAVLEIMPYPGGLE-----RNIQQCLRD 200
Cdd:PRK06292  158 tsDDAF---------ELDKL-PKSLAVI-GGGVIGLELGqalSRL---GVKV-TVFERGDRILPLEdpevsKQAQKILSK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 201 fNIPLYLSHTVTAIEgEKRLEKVIASQVDykwnpipGTEKVFDVDMLITSVGLIPSTKPVDFVDA-----DPGFLVSN-T 274
Cdd:PRK06292  223 -EFKIKLGAKVTSVE-KSGDEKVEELEKG-------GKTETIEADYVLVATGRRPNTDGLGLENTgieldERGRPVVDeH 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1131021033 275 NQTSEDWIFAAGNCTVIFDLVDFVAKEGEKAGKYAALYAQGK 316
Cdd:PRK06292  294 TQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAGG 335
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
153-226 5.36e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 38.34  E-value: 5.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131021033 153 KAVILGSGDIGLIMARRLTLEGIKVEaVLEIMPYPGGLE-----RNIQQCLRDFNIPLYLSHTVTAIEGEKRLEKVIAS 226
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVT-VVERRDRLLPGFdpeiaKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
7-316 6.15e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 42.02  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033   7 VVIIGGGAAGMAAAYSATREGADVILLERDEDTGGVLNQCIhngfglhyfkkdltgPEFK---ELAKERIKDLNILYGTY 83
Cdd:PRK12814  196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGI---------------PRFRlpeSVIDADIAPLRAMGAEF 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033  84 VLEVTKDKRIIFVDRRGIHEietkALVMATGARERhfNSLPVPGKRITGVfTAGLA-QRFINL-ENLKPGNKAVILGSGD 161
Cdd:PRK12814  261 RFNTVFGRDITLEELQKEFD----AVLLAVGAQKA--SKMGIPGEELPGV-ISGIDfLRNVALgTALHPGKKVVVIGGGN 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 162 IGLIMAR---RLTLEGIKV--EAVLEIMPyPGGLErnIQQCLRDfNIPLYLSHTVTAIE-GEKRLE----KVIASQVD-- 229
Cdd:PRK12814  334 TAIDAARtalRLGAESVTIlyRRTREEMP-ANRAE--IEEALAE-GVSLRELAAPVSIErSEGGLEltaiKMQQGEPDes 409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 230 --YKWNPIPGTEKVFDVDMLITSVG--LIPSTKPVDFVDADPGFLVSN---TNQTSEDWIFAAGNCTVIFDLVDFVAKEG 302
Cdd:PRK12814  410 grRRPVPVEGSEFTLQADTVISAIGqqVDPPIAEAAGIGTSRNGTVKVdpeTLQTSVAGVFAGGDCVTGADIAINAVEQG 489
                         330
                  ....*....|....
gi 1131021033 303 EKAGKYAALYAQGK 316
Cdd:PRK12814  490 KRAAHAIDLFLNGK 503
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
234-316 1.70e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 40.36  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131021033 234 PIPGTEKVFDVDMLITSVGLIPsTKPVDF------VDADPGFLVSNTNQTSEDWIFAAGNCTVIFDLVDFVAKEGEKAGK 307
Cdd:PRK12770  265 PIPGSEFVLEADTVVFAIGEIP-TPPFAKeclgieLNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQ 343

                  ....*....
gi 1131021033 308 YAALYAQGK 316
Cdd:PRK12770  344 SIHEWLDLK 352
 
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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