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Entry: A0A0D6ST67_9PSED
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ID   A0A0D6ST67_9PSED        Unreviewed;       182 AA.
AC   A0A0D6ST67;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=SZ55_2381 {ECO:0000313|EMBL:KIV71558.1};
OS   Pseudomonas sp. FeS53a.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV71558.1, ECO:0000313|Proteomes:UP000032531};
RN   [1] {ECO:0000313|EMBL:KIV71558.1, ECO:0000313|Proteomes:UP000032531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FeS53a {ECO:0000313|EMBL:KIV71558.1,
RC   ECO:0000313|Proteomes:UP000032531};
RA   de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA   Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT   "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT   stressed soils.";
RL   Submitted (JAN-2015) 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 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:KIV71558.1}.
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DR   EMBL; JYFT01000040; KIV71558.1; -; Genomic_DNA.
DR   RefSeq; WP_044405822.1; NZ_JYFT01000040.1.
DR   AlphaFoldDB; A0A0D6ST67; -.
DR   GeneID; 57397385; -.
DR   PATRIC; fig|1604022.3.peg.3572; -.
DR   Proteomes; UP000032531; 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:KIV71558.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01351};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000313|EMBL:KIV71558.1}.
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;  20623 MW;  5E9A24AEF31F634E CRC64;
     MIKYIYDVVA GTFTQLRSLV MVFSHGFRKR DTLQYPEEPV YLPPRYRGRI VLTRDPDGEE
     RCVACNLCAV ACPVGCISLQ KAETEDGRWY PEFFRINFSR CIFCGLCEEA CPTTAIQLTP
     DFEMGEYKRQ DLVYEKEDLL ISGPGKNPDY NFYRVAGMAI AGKPKGAAQN EAEPINVKSL
     LP
//
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