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Database: UniProt
Entry: W6M938_9GAMM
LinkDB: W6M938_9GAMM
Original site: W6M938_9GAMM 
ID   W6M938_9GAMM            Unreviewed;       167 AA.
AC   W6M938;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000256|ARBA:ARBA00040641, ECO:0000256|HAMAP-Rule:MF_01351};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01351};
DE   AltName: Full=NADH dehydrogenase I subunit I {ECO:0000256|ARBA:ARBA00041748, ECO:0000256|HAMAP-Rule:MF_01351};
DE   AltName: Full=NDH-1 subunit I {ECO:0000256|ARBA:ARBA00043079, ECO:0000256|HAMAP-Rule:MF_01351};
GN   Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351,
GN   ECO:0000313|EMBL:CDI03109.1};
GN   ORFNames=BN873_380091 {ECO:0000313|EMBL:CDI03109.1};
OS   Candidatus Competibacter denitrificans Run_A_D11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria;
OC   Candidatus Competibacteraceae; Candidatus Competibacter.
OX   NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI03109.1, ECO:0000313|Proteomes:UP000035760};
RN   [1] {ECO:0000313|EMBL:CDI03109.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI03109.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI03109.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI03109.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA   Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT   "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT   functional metabolic diversity.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01351}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01351};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000256|ARBA:ARBA00038844}.
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01351}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01351}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00010277, ECO:0000256|HAMAP-Rule:MF_01351}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDI03109.1}.
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DR   EMBL; CBTJ020000045; CDI03109.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6M938; -.
DR   STRING; 1400863.BN873_380091; -.
DR   Proteomes; UP000035760; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.3270; -; 1.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   NCBIfam; TIGR01971; NuoI; 1.
DR   PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01351};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01351};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01351}; Membrane {ECO:0000256|HAMAP-Rule:MF_01351};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01351}; NAD {ECO:0000256|HAMAP-Rule:MF_01351};
KW   Oxidoreductase {ECO:0000313|EMBL:CDI03109.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01351}; Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}.
FT   DOMAIN          58..88
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          98..127
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         107
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         110
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01351"
SQ   SEQUENCE   167 AA;  19283 MW;  CC2E23F9D19BF079 CRC64;
     MAMNTLNTVR HYFKTFLLWE LLLGLRVTGR YLFAKKLTVQ YPEELTPLSH RFRGLHAQRR
     YPNGEERCIA CKLCEAVCPA LAITIESEQR ADGSRRTVRY DIDLFKCIYC GFCEEACPVD
     AIVETRTFAY HFENRGEHIM TKEKLLAHGD LCEAQIAADR AIDAAYR
//
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