NUOI_PECAS
ID NUOI_PECAS Reviewed; 180 AA.
AC Q6D2S4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NDH-1 subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
GN Name=nuoI {ECO:0000255|HAMAP-Rule:MF_01351}; OrderedLocusNames=ECA3021;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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:0000255|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:0000255|HAMAP-Rule:MF_01351};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01351}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01351}.
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DR EMBL; BX950851; CAG75920.1; -; Genomic_DNA.
DR RefSeq; WP_005969838.1; NC_004547.2.
DR AlphaFoldDB; Q6D2S4; -.
DR SMR; Q6D2S4; -.
DR STRING; 218491.ECA3021; -.
DR EnsemblBacteria; CAG75920; CAG75920; ECA3021.
DR GeneID; 57209708; -.
DR KEGG; eca:ECA3021; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_3_6; -.
DR OMA; RGDLYYT; -.
DR OrthoDB; 1619561at2; -.
DR Proteomes; UP000007966; 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 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 PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Reference proteome; Repeat; Translocase;
KW Ubiquinone.
FT CHAIN 1..180
FT /note="NADH-quinone oxidoreductase subunit I"
FT /id="PRO_0000245705"
FT DOMAIN 50..80
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT DOMAIN 90..119
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
SQ SEQUENCE 180 AA; 20373 MW; 54B749903EBD58E5 CRC64;
MTLKELVVGF GTQIRSICMV GSNAFKKRET RMYPEEPVNP PPRYRGRIVL TRDPDGEERC
VACNLCAVAC PVGCISLQKA ETKDGRWYPE FFRVNFSRCI FCGFCEEACP TTAIQLTPDF
EMGEYKRQDL VYEKEDLLIS GPGKYPEYNF YRMAGMAIDG KDKGEAENEA KPIDVKGLLP
