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Conserved domains on  [gi|488308239|ref|WP_002377959|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Bacillota]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 10617647)

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; belongs to the pyridine nucleotide-disulfide oxidoreductase family

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0016491
PubMed:  30945211

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
22-315 3.24e-124

Pyridine nucleotide-disulphide oxidoreductase;


:

Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 360.00  E-value: 3.24e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239   22 LKDFGINNFAILERKQVGNSFIKWPEQTRFITPSFTSNGFGMPDLNAIAIDTSPSYTLGEERLSGKDYAKYLQLVSEEYK 101
Cdd:pfam13738  10 LKKAGLEDYLILEKGNIGNSFYRYPTHMTFFSPSFTSNGFGIPDLNAISPGTSPAFTFNREHPSGNEYAEYLRRVADHFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  102 LPIKTNCKVQSIKKEKTGYLLETTKGFIYAEYVIFAMGEFSFPNKSSIKgayKNSLHYGEINSWIEIKGDKQTIIGGNES 181
Cdd:pfam13738  90 LPINLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP---ELPKHYSYVKDFHPYAGQKVVVIGGYNS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  182 AIDAAIELAKLGKRVTIYTDTLGLNIRDADPSKRLAPRTRQRFFDLRVNQKkldsIKIYTTTKVKKIEKKSTSYILITEN 261
Cdd:pfam13738 167 AVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLSPDTLNRLEELVKNGK----IKAHFNAEVKEITEVDVSYKVHTED 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488308239  262 GKSLPVENIPILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIAKNIFLTG 315
Cdd:pfam13738 243 GRKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEETESTNVPGLFLAG 296
 
Name Accession Description Interval E-value
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
22-315 3.24e-124

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 360.00  E-value: 3.24e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239   22 LKDFGINNFAILERKQVGNSFIKWPEQTRFITPSFTSNGFGMPDLNAIAIDTSPSYTLGEERLSGKDYAKYLQLVSEEYK 101
Cdd:pfam13738  10 LKKAGLEDYLILEKGNIGNSFYRYPTHMTFFSPSFTSNGFGIPDLNAISPGTSPAFTFNREHPSGNEYAEYLRRVADHFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  102 LPIKTNCKVQSIKKEKTGYLLETTKGFIYAEYVIFAMGEFSFPNKSSIKgayKNSLHYGEINSWIEIKGDKQTIIGGNES 181
Cdd:pfam13738  90 LPINLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP---ELPKHYSYVKDFHPYAGQKVVVIGGYNS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  182 AIDAAIELAKLGKRVTIYTDTLGLNIRDADPSKRLAPRTRQRFFDLRVNQKkldsIKIYTTTKVKKIEKKSTSYILITEN 261
Cdd:pfam13738 167 AVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLSPDTLNRLEELVKNGK----IKAHFNAEVKEITEVDVSYKVHTED 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488308239  262 GKSLPVENIPILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIAKNIFLTG 315
Cdd:pfam13738 243 GRKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEETESTNVPGLFLAG 296
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
29-344 6.06e-17

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 80.55  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  29 NFAILERKQVGNSFIKWPEqtrfitpsfTSNGFGMPdlnaiaidtspsytlgeERLSGKDYAKYLQLVSEEYKLPIKTnC 108
Cdd:COG0492   25 KTLVIEGGEPGGQLATTKE---------IENYPGFP-----------------EGISGPELAERLREQAERFGAEILL-E 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 109 KVQSIKKEKTGYLLETTKGFIY-AEYVIFAMGefSFPNKSSIKGAYK---NSLHYGEINSWIEIKGDKQTIIGGNESAID 184
Cdd:COG0492   78 EVTSVDKDDGPFRVTTDDGTEYeAKAVIIATG--AGPRKLGLPGEEEfegRGVSYCATCDGFFFRGKDVVVVGGGDSALE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 185 AAIELAKLGKRVTIYT--DTLglnirdadpskRLAPRTRQRFFDlrvnqkkLDSIKIYTTTKVKKIEKKS--TSyiLITE 260
Cdd:COG0492  156 EALYLTKFASKVTLIHrrDEL-----------RASKILVERLRA-------NPKIEVLWNTEVTEIEGDGrvEG--VTLK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 261 NGKSLPVENIP----ILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIAkNIFLTGpNVRKgntifcyiYKFRQRF- 335
Cdd:COG0492  216 NVKTGEEKELEvdgvFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVP-GVFAAG-DVRD--------YKYRQAAt 285
                        330
                 ....*....|....
gi 488308239 336 -----AVIANEIAR 344
Cdd:COG0492  286 aagegAIAALSAAR 299
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
174-315 1.87e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 46.57  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 174 TIIGGNESAIDAAIELAKLGKRVTIYtdtlglnirdaDPSKRLAPRT-RQRFFDLRVNQKKLDSIKIYTTTKVKKIEKKS 252
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRII-----------QLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGED 221
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488308239 253 TSYILITENGKSlpVENIPILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIaKNIFLTG 315
Cdd:PRK09564 222 KVEGVVTDKGEY--EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSI-ENIYAAG 281
 
Name Accession Description Interval E-value
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
22-315 3.24e-124

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 360.00  E-value: 3.24e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239   22 LKDFGINNFAILERKQVGNSFIKWPEQTRFITPSFTSNGFGMPDLNAIAIDTSPSYTLGEERLSGKDYAKYLQLVSEEYK 101
Cdd:pfam13738  10 LKKAGLEDYLILEKGNIGNSFYRYPTHMTFFSPSFTSNGFGIPDLNAISPGTSPAFTFNREHPSGNEYAEYLRRVADHFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  102 LPIKTNCKVQSIKKEKTGYLLETTKGFIYAEYVIFAMGEFSFPNKSSIKgayKNSLHYGEINSWIEIKGDKQTIIGGNES 181
Cdd:pfam13738  90 LPINLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP---ELPKHYSYVKDFHPYAGQKVVVIGGYNS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  182 AIDAAIELAKLGKRVTIYTDTLGLNIRDADPSKRLAPRTRQRFFDLRVNQKkldsIKIYTTTKVKKIEKKSTSYILITEN 261
Cdd:pfam13738 167 AVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLSPDTLNRLEELVKNGK----IKAHFNAEVKEITEVDVSYKVHTED 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488308239  262 GKSLPVENIPILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIAKNIFLTG 315
Cdd:pfam13738 243 GRKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEETESTNVPGLFLAG 296
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
29-344 6.06e-17

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 80.55  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  29 NFAILERKQVGNSFIKWPEqtrfitpsfTSNGFGMPdlnaiaidtspsytlgeERLSGKDYAKYLQLVSEEYKLPIKTnC 108
Cdd:COG0492   25 KTLVIEGGEPGGQLATTKE---------IENYPGFP-----------------EGISGPELAERLREQAERFGAEILL-E 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 109 KVQSIKKEKTGYLLETTKGFIY-AEYVIFAMGefSFPNKSSIKGAYK---NSLHYGEINSWIEIKGDKQTIIGGNESAID 184
Cdd:COG0492   78 EVTSVDKDDGPFRVTTDDGTEYeAKAVIIATG--AGPRKLGLPGEEEfegRGVSYCATCDGFFFRGKDVVVVGGGDSALE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 185 AAIELAKLGKRVTIYT--DTLglnirdadpskRLAPRTRQRFFDlrvnqkkLDSIKIYTTTKVKKIEKKS--TSyiLITE 260
Cdd:COG0492  156 EALYLTKFASKVTLIHrrDEL-----------RASKILVERLRA-------NPKIEVLWNTEVTEIEGDGrvEG--VTLK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 261 NGKSLPVENIP----ILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIAkNIFLTGpNVRKgntifcyiYKFRQRF- 335
Cdd:COG0492  216 NVKTGEEKELEvdgvFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVP-GVFAAG-DVRD--------YKYRQAAt 285
                        330
                 ....*....|....
gi 488308239 336 -----AVIANEIAR 344
Cdd:COG0492  286 aagegAIAALSAAR 299
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
80-315 3.69e-16

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: 78.13  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239   80 GEERLSGKDYAKYLQLVSEEYKLPIKTNCKVQSIKKEK-----TGYLLETTKGFIY-AEYVIFAMGefSFPNKSSIKGAY 153
Cdd:pfam07992  53 PEIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPgakkvVLEELVDGDGETItYDRLVIATG--ARPRLPPIPGVE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  154 KNSLHYGEI----NSWIEIKGDKQ-TIIGGNESAIDAAIELAKLGKRVTIYTDTLGLNiRDADPskRLAPRTRQRFfdlr 228
Cdd:pfam07992 131 LNVGFLVRTldsaEALRLKLLPKRvVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL-RAFDE--EISAALEKAL---- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  229 vnqkKLDSIKIYTTTKVKKIEKKSTSYILITENGKSLPVENIpILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIa 308
Cdd:pfam07992 204 ----EKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLV-VVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSV- 277

                  ....*..
gi 488308239  309 KNIFLTG 315
Cdd:pfam07992 278 PGIYAAG 284
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
20-202 3.93e-09

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: 57.95  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  20 VALKDFGInNFAILERK-QVGNSfikWPEQT----RFITPSFTSN--GFGMPdlnaiaiDTSPSYTLGEErlsgkdYAKY 92
Cdd:COG2072   23 YHLRRAGI-DFVVLEKAdDVGGT---WRDNRypglRLDTPSHLYSlpFFPNW-------SDDPDFPTGDE------ILAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  93 LQLVSEEYKL--PIKTNCKVQSI--KKEKTGYLLETTKGFIY-AEYVIFAMGEFSFPNKSSIKG------------AYKN 155
Cdd:COG2072   86 LEAYADKFGLrrPIRFGTEVTSArwDEADGRWTVTTDDGETLtARFVVVATGPLSRPKIPDIPGledfageqlhsaDWRN 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488308239 156 SLHYgeinswieiKGDKQTIIGGNESAIDAAIELAKLGKRVTIYTDT 202
Cdd:COG2072  166 PVDL---------AGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
174-315 1.87e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 46.57  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 174 TIIGGNESAIDAAIELAKLGKRVTIYtdtlglnirdaDPSKRLAPRT-RQRFFDLRVNQKKLDSIKIYTTTKVKKIEKKS 252
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRII-----------QLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGED 221
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488308239 253 TSYILITENGKSlpVENIPILCTGFKNGTKSITASLFKYKENGEVLLNDFDESTIaKNIFLTG 315
Cdd:PRK09564 222 KVEGVVTDKGEY--EADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSI-ENIYAAG 281
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
175-262 2.51e-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: 39.11  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  175 IIGGNESAIDAAIELAKLGKRVTI--YTDTLgLNIRDADPSKRLAPRTRQRffdlrvnqkkldSIKIYTTTKVKKIEKKS 252
Cdd:pfam00070   4 VVGGGYIGLELAGALARLGSKVTVveRRDRL-LPGFDPEIAKILQEKLEKN------------GIEFLLNTTVEAIEGNG 70
                          90
                  ....*....|
gi 488308239  253 TSYILITENG 262
Cdd:pfam00070  71 DGVVVVLTDG 80
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
175-279 3.17e-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: 39.22  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239  175 IIGGNESAIDAAIELAKLGKRVTIYTDTLGLNIRDADPSKRL-----APRTRQRFFDLRVNQKKLDS-----IKIYTTTK 244
Cdd:pfam07992   5 VIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYGGCVLSKALlgaaeAPEIASLWADLYKRKEEVVKklnngIEVLLGTE 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488308239  245 VKKIEKKSTSYIL---ITENGKSLPVENIpILCTGFKN 279
Cdd:pfam07992  85 VVSIDPGAKKVVLeelVDGDGETITYDRL-VIATGARP 121
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
175-278 6.80e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.30  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488308239 175 IIGGNESAIDAAIELAKLGKRVTIY--TDTLGLNIR--------DADPSKRLAPRTRqrffdlRVNQKKLdsIKIYTTTK 244
Cdd:COG1148  145 VIGGGIAGMTAALELAEQGYEVYLVekEPELGGRAAqlhktfpgLDCPQCILEPLIA------EVEANPN--ITVYTGAE 216
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488308239 245 VKKIEKKSTSYILITENG----KSLPVENIpILCTGFK 278
Cdd:COG1148  217 VEEVSGYVGNFTVTIKKGpreeIEIEVGAI-VLATGFK 253
 
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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