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Conserved domains on  [gi|547883134|ref|WP_022288457|]
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MULTISPECIES: NAD(P)H-dependent oxidoreductase subunit E [Oscillospiraceae]

Protein Classification

complex I 24 kDa subunit family protein( domain architecture ID 11112961)

complex I 24 kDa subunit family protein is a thioredoxin-like ferredoxin subunit of an NADH dehydrogenase is involved in the reversible oxidation of molecular hydrogen using NADH or NADPH as electron donor or acceptor; such as bacterial NADH-quinone oxidoreductase subunit E (NuoE) and eukaryotic NADH-ubiquinone oxidoreductase 24 kDa subunit

EC:  7.1.1.-
Gene Ontology:  GO:0051537|GO:0016491
PubMed:  15916556|30277212

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
2Fe-2S_thioredx pfam01257
Thioredoxin-like [2Fe-2S] ferredoxin;
10-153 1.89e-63

Thioredoxin-like [2Fe-2S] ferredoxin;


:

Pssm-ID: 460139  Cd Length: 145  Bit Score: 191.15  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134   10 IDKILENH--EKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:pfam01257   1 IKEIIAKYprKRSALIPILHLAQEEYGYLPPEAIEYVAELLGIPPARVYEVATFYTMFSLKPVGKYHIQVCTGTPCHLRG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883134   88 SIPILEYLRGELGLSEKKtTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:pfam01257  81 SDEILEALEKKLGIKPGE-TTPDGKFTLEEVECLGACDNAPVMQINDDYYGDLTPEKVDEILEELK 145
 
Name Accession Description Interval E-value
2Fe-2S_thioredx pfam01257
Thioredoxin-like [2Fe-2S] ferredoxin;
10-153 1.89e-63

Thioredoxin-like [2Fe-2S] ferredoxin;


Pssm-ID: 460139  Cd Length: 145  Bit Score: 191.15  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134   10 IDKILENH--EKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:pfam01257   1 IKEIIAKYprKRSALIPILHLAQEEYGYLPPEAIEYVAELLGIPPARVYEVATFYTMFSLKPVGKYHIQVCTGTPCHLRG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883134   88 SIPILEYLRGELGLSEKKtTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:pfam01257  81 SDEILEALEKKLGIKPGE-TTPDGKFTLEEVECLGACDNAPVMQINDDYYGDLTPEKVDEILEELK 145
NuoE COG1905
NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; ...
 10-154 1.74e-62

NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441509  Cd Length: 159  Bit Score: 189.20  E-value: 1.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENH--EKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:COG1905   14 IDEIIAKYprKRSALIPILHLVQEEFGYLPEEAIEEIAEALGLPPAEVYGVATFYSMFRLKPVGKHVIRVCTGTACHLRG 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547883134  88 SIPILEYLRGELGLSEKKtTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELRE 154
Cdd:COG1905   94 AEELLEALEEKLGIKPGE-TTADGKFTLEEVECLGACGLAPVMMVNDDVYGRLTPEKVDEILDELRA 159
PRK07539 PRK07539
NADH-quinone oxidoreductase subunit NuoE;
10-153 1.02e-39

NADH-quinone oxidoreductase subunit NuoE;


Pssm-ID: 181024  Cd Length: 154  Bit Score: 131.43  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENHE--KTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:PRK07539  10 IEREIAKYPrpRSAVIPALKIVQEQRGWVPDEAIEAVADYLGMPAIDVEEVATFYSMIFRQPVGRHVIQVCTSTPCWLRG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883134  88 SIPILEYLRGELGLsEKKTTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:PRK07539  90 GEAILAALKKKLGI-KPGETTADGRFTLLEVECLGACDNAPVVMINDDTYEDLTPEKIDELLDELK 154
nuoE_fam TIGR01958
NADH-quinone oxidoreductase, E subunit; This model describes the E chain of complexes that ...
 10-153 1.13e-33

NADH-quinone oxidoreductase, E subunit; This model describes the E chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoB. This model does not identify proteins from chloroplast and cyanobacteria. [Energy metabolism, Electron transport]


Pssm-ID: 131013  Cd Length: 148  Bit Score: 115.55  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134   10 IDKILENHEKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRKSI 89
Cdd:TIGR01958   6 IAKYPDDQKRSAIMPALMIAQEQKGWVTPEAIAAVAEMLGIPPVWVYEVATFYSMFDTEPVGRYHLQVCTNVPCALRGSE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547883134   90 PILEYLRGELGlSEKKTTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:TIGR01958  86 ALLKYLENKLG-IKPGETTPDGRFTLVEVECLGACGNAPVMMINDDYYEFLTPEKLDELLERYE 148
TRX_Fd_NuoE cd03064
TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E ...
 72-152 1.52e-29

TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily; Nuo, also called respiratory chain Complex 1, is the entry point for electrons into the respiratory chains of bacteria and the mitochondria of eukaryotes. It is a multisubunit complex with at least 14 core subunits. It catalyzes the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane, providing the proton motive force required for energy-consuming processes. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE core subunit, also called the 24 kD subunit of Complex 1. This subfamily also include formate dehydrogenases, NiFe hydrogenases and NAD-reducing hydrogenases, that contain a NuoE domain. A subset of these proteins contain both NuoE and NuoF in a single chain. NuoF, also called the 51 kD subunit of Complex 1, contains one [4Fe-4S] cluster and also binds the NADH substrate and FMN.


Pssm-ID: 239362 [Multi-domain]  Cd Length: 80  Bit Score: 102.98  E-value: 1.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  72 KYVIKCCDGTACHVRKSIPILEYLRGELGLSEKKTTtDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKE 151
Cdd:cd03064    1 KHVIRVCTGTACHLRGAEALLEALEKKLGIKPGETT-PDGRFTLEEVECLGACDLAPVMMINDDVYGRLTPEKVDAILEA 79


                 .
gi 547883134 152 L 152
Cdd:cd03064   80 L 80
 
Name Accession Description Interval E-value
2Fe-2S_thioredx pfam01257
Thioredoxin-like [2Fe-2S] ferredoxin;
10-153 1.89e-63

Thioredoxin-like [2Fe-2S] ferredoxin;


Pssm-ID: 460139  Cd Length: 145  Bit Score: 191.15  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134   10 IDKILENH--EKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:pfam01257   1 IKEIIAKYprKRSALIPILHLAQEEYGYLPPEAIEYVAELLGIPPARVYEVATFYTMFSLKPVGKYHIQVCTGTPCHLRG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883134   88 SIPILEYLRGELGLSEKKtTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:pfam01257  81 SDEILEALEKKLGIKPGE-TTPDGKFTLEEVECLGACDNAPVMQINDDYYGDLTPEKVDEILEELK 145
NuoE COG1905
NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; ...
 10-154 1.74e-62

NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441509  Cd Length: 159  Bit Score: 189.20  E-value: 1.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENH--EKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:COG1905   14 IDEIIAKYprKRSALIPILHLVQEEFGYLPEEAIEEIAEALGLPPAEVYGVATFYSMFRLKPVGKHVIRVCTGTACHLRG 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547883134  88 SIPILEYLRGELGLSEKKtTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELRE 154
Cdd:COG1905   94 AEELLEALEEKLGIKPGE-TTADGKFTLEEVECLGACGLAPVMMVNDDVYGRLTPEKVDEILDELRA 159
PRK07539 PRK07539
NADH-quinone oxidoreductase subunit NuoE;
10-153 1.02e-39

NADH-quinone oxidoreductase subunit NuoE;


Pssm-ID: 181024  Cd Length: 154  Bit Score: 131.43  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENHE--KTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:PRK07539  10 IEREIAKYPrpRSAVIPALKIVQEQRGWVPDEAIEAVADYLGMPAIDVEEVATFYSMIFRQPVGRHVIQVCTSTPCWLRG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883134  88 SIPILEYLRGELGLsEKKTTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:PRK07539  90 GEAILAALKKKLGI-KPGETTADGRFTLLEVECLGACDNAPVVMINDDTYEDLTPEKIDELLDELK 154
PRK07571 PRK07571
bidirectional hydrogenase complex protein HoxE; Reviewed
 21-154 3.58e-35

bidirectional hydrogenase complex protein HoxE; Reviewed


Pssm-ID: 236053  Cd Length: 169  Bit Score: 120.24  E-value: 3.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  21 AVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRKSIPILEYLRGELG 100
Cdd:PRK07571  37 ALIEVLHKAQELFGYLERDLLLYVARQLKLPLSRVYGVATFYHLFSLKPSGEHTCVVCTGTACYVKGSAAILEDLENELG 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 547883134 101 LSEKKTTTDDLMfTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELRE 154
Cdd:PRK07571 117 IKAGETTADGKL-SLLTARCLGACGIAPAVVFDGKVAGKQTPESVLEKVQGWLQ 169
nuoE_fam TIGR01958
NADH-quinone oxidoreductase, E subunit; This model describes the E chain of complexes that ...
 10-153 1.13e-33

NADH-quinone oxidoreductase, E subunit; This model describes the E chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoB. This model does not identify proteins from chloroplast and cyanobacteria. [Energy metabolism, Electron transport]


Pssm-ID: 131013  Cd Length: 148  Bit Score: 115.55  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134   10 IDKILENHEKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRKSI 89
Cdd:TIGR01958   6 IAKYPDDQKRSAIMPALMIAQEQKGWVTPEAIAAVAEMLGIPPVWVYEVATFYSMFDTEPVGRYHLQVCTNVPCALRGSE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547883134   90 PILEYLRGELGlSEKKTTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELR 153
Cdd:TIGR01958  86 ALLKYLENKLG-IKPGETTPDGRFTLVEVECLGACGNAPVMMINDDYYEFLTPEKLDELLERYE 148
TRX_Fd_NuoE cd03064
TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E ...
 72-152 1.52e-29

TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily; Nuo, also called respiratory chain Complex 1, is the entry point for electrons into the respiratory chains of bacteria and the mitochondria of eukaryotes. It is a multisubunit complex with at least 14 core subunits. It catalyzes the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane, providing the proton motive force required for energy-consuming processes. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE core subunit, also called the 24 kD subunit of Complex 1. This subfamily also include formate dehydrogenases, NiFe hydrogenases and NAD-reducing hydrogenases, that contain a NuoE domain. A subset of these proteins contain both NuoE and NuoF in a single chain. NuoF, also called the 51 kD subunit of Complex 1, contains one [4Fe-4S] cluster and also binds the NADH substrate and FMN.


Pssm-ID: 239362 [Multi-domain]  Cd Length: 80  Bit Score: 102.98  E-value: 1.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  72 KYVIKCCDGTACHVRKSIPILEYLRGELGLSEKKTTtDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKE 151
Cdd:cd03064    1 KHVIRVCTGTACHLRGAEALLEALEKKLGIKPGETT-PDGRFTLEEVECLGACDLAPVMMINDDVYGRLTPEKVDAILEA 79


                 .
gi 547883134 152 L 152
Cdd:cd03064   80 L 80
PRK05988 PRK05988
formate dehydrogenase subunit gamma; Validated
 10-154 1.37e-27

formate dehydrogenase subunit gamma; Validated


Pssm-ID: 180339  Cd Length: 156  Bit Score: 100.42  E-value: 1.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENHEKT--AVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYVIKCCDGTACHVRK 87
Cdd:PRK05988  11 IAAIIAEHKHLegALLPILHAIQDEFGYVPEDAVPVIAEALNLSRAEVHGVITFYHDFRTHPPGRHVLKLCRAEACQAMG 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547883134  88 SIPILEYLRGELGLSEKKTTTDDlMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKELRE 154
Cdd:PRK05988  91 GDALAAHAKARLGIDFHQTTADG-AVTLEPVYCLGLCACSPAAMLDGEVHGRLDPQRLDALLAEARR 156
TRX_Fd_family cd02980
Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX ...
 73-152 6.85e-19

Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers.


Pssm-ID: 239278 [Multi-domain]  Cd Length: 77  Bit Score: 75.74  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  73 YVIKCCDGTACHVRKSIPILEYLRGELGLSEKktttdDLMFTVETVSCLGACGLAPVLTVN--DVVHPEMNPDKAAALLK 150
Cdd:cd02980    1 HHILVCTGTACGLRGAEELLEALEKELGIRGG-----DGRVTVERVGCLGACGLAPVVVVYpdGVWYGRVTPEDVEEIVE 75


                 ..
gi 547883134 151 EL 152
Cdd:cd02980   76 EL 77
TRX_Fd_NuoE_FDH_gamma cd03081
TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E ...
 72-152 2.86e-13

TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily, NAD-dependent formate dehydrogenase (FDH) gamma subunit; composed of proteins similar to the gamma subunit of NAD-linked FDH of Ralstonia eutropha, a soluble enzyme that catalyzes the irreversible oxidation of formate to carbon dioxide accompanied by the reduction of NAD+ to NADH. FDH is a heteromeric enzyme composed of four nonidentical subunits (alpha, beta, gamma and delta). The FDH gamma subunit is closely related to NuoE, which is part of a multisubunit complex (Nuo) catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE. Similarly, the FDH gamma subunit is hypothesized to be involved in an electron transport chain involving other FDH subunits, upon the oxidation of formate.


Pssm-ID: 239379  Cd Length: 80  Bit Score: 61.24  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  72 KYVIKCCDGTACHVRKSIPILEYLRGELGLSEKKTTTDDlMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKE 151
Cdd:cd03081    1 RHVLKLCRAEACQAMGAEALAAHIKARLGIDFHETTADG-SVTLEPVYCLGLCACSPAAMIDGEVHGRVDPEKFDALLAE 79


                 .
gi 547883134 152 L 152
Cdd:cd03081   80 L 80
PRK12373 PRK12373
NADH-quinone oxidoreductase subunit E;
10-152 1.84e-11

NADH-quinone oxidoreductase subunit E;


Pssm-ID: 237082 [Multi-domain]  Cd Length: 400  Bit Score: 60.59  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  10 IDKILENHEKTAVIAILQDIQEIYHYLPKEIFPYLAKKLGTGEARIYSVATFYENFSLEPKGKYV-IKCCDGTACHVRKS 88
Cdd:PRK12373  27 ITKYPEGRQASAVIPLLMRAQEQEGWVTRAAIEKVADMLDMAYIRVLEVATFYTQFQLQPVGTRAhIQVCGTTPCMLRGS 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547883134  89 IPILEYLRGELGlSEKKTTTDDLMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKEL 152
Cdd:PRK12373 107 EALMAVCKSKIH-AHPHELNADGTLSWEEVECLGACVNAPMVQIGKDYYEDLTPERLEEIIDAF 169
TRX_Fd_NuoE_hoxF cd03083
TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E ...
 72-152 2.47e-06

TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily, hoxF; composed of proteins similar to the NAD-reducing hydrogenase (hoxS) alpha subunit of Alcaligenes eutrophus H16. HoxS is a cytoplasmic hydrogenase catalyzing the oxidation of molecular hydrogen accompanied by the reduction of NAD. It is composed of four structural subunits encoded by the genes hoxF, hoxU, hoxY and hoxH. The hoxF protein (or alpha subunit) is a fusion protein containing an N-terminal NuoE-like domain and a C-terminal NuoF domain. NuoE and NuoF are components of Nuo, a multisubunit complex catalyzing the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster in NuoE and the [4Fe-4S] cluster in NuoF. In addition, NuoF is also the NADH- and FMN-binding subunit. HoxF may be involved in the electron transport chain during the NAD-dependent oxidation of hydrogen through its NuoF domain. The NuoE-like domain of hoxF contains only one conserved cysteine in its putative active site, compared to four cysteines in NuoE, and may have lost the ability to bind [2Fe-2S] clusters.


Pssm-ID: 239381  Cd Length: 80  Bit Score: 43.17  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  72 KYVIKCCDGTACHVRKSIPILEYLRGELGLSEKKTTTDDlMFTVETVSCLGACGLAPVLTVNDVVHPEMNPDKAAALLKE 151
Cdd:cd03083    1 KYRIYLSDSITDRMNGYKAVLDALCRELGIRFGEVDEDG-MVGLFFTSCTGLCDQGPALLINNRVFTRLTPGRIDQIAEL 79


                 .
gi 547883134 152 L 152
Cdd:cd03083   80 I 80
COG3411 COG3411
2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway ...
 69-151 7.51e-06

2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway/BioSystem: 2Fe2S


Pssm-ID: 442637  Cd Length: 96  Bit Score: 42.19  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883134  69 PKGKYVIKCCDGTaCHVRKSIPILEYLRGEL---GLSEKktttddlmFTVETVSCLGACGLAPVLtvndVVHPE------ 139
Cdd:COG3411    2 SKYRHHVLVCTGS-CGAAGAEEVLDALKEELkerGLDGD--------VRVTKTGCLGRCEQGPVV----VVYPEgvwygn 68

                         90
                 ....*....|..
gi 547883134 140 MNPDKAAALLKE 151
Cdd:COG3411   69 VTPEDVPEIVEE 80
 
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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