ID C3JY88_PSEFS Unreviewed; 182 AA.
AC C3JY88;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 108.
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 OrderedLocusNames=PFLU_3825 {ECO:0000313|EMBL:CAY50146.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY50146.1};
RN [1] {ECO:0000313|EMBL:CAY50146.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY50146.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2798023.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2798023.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) 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, ECO:0000256|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01351}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01351}.
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DR EMBL; OV986001; CAI2798023.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY50146.1; -; Genomic_DNA.
DR RefSeq; WP_003174725.1; NC_012660.1.
DR AlphaFoldDB; C3JY88; -.
DR STRING; 294.SRM1_03452; -.
DR GeneID; 78552532; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_3_6; -.
DR OrthoDB; 9808559at2; -.
DR Proteomes; UP001152918; Chromosome.
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; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10849:SF35; NADH-QUINONE OXIDOREDUCTASE SUBUNIT I; 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 inner membrane {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:CAY50146.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}.
FT DOMAIN 52..82
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 92..121
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 62
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 65
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 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 72
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 101
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 104
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 111
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 182 AA; 20446 MW; 4B1F1BF463B57881 CRC64;
MFKYIGDIVK GTGTQLRSLV MVFGHGFRKR DTLQYPEEAV YLPPRYRGRI VLTRDPDGEE
RCVACNLCAV ACPVGCISLQ KAETEDGRWY PDFFRINFSR CIFCGLCEEA CPTTAIQLTP
DFEMAEFKRQ DLVYEKEDLL ISGPGKNPDY NFYRVAGMAV AGKPKGAAQN EAEPINVKSL
LP
//
