ID I7HEM8_9HELI Unreviewed; 234 AA.
AC I7HEM8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=NADH-quinone oxidoreductase subunit I {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|HAMAP-Rule:MF_01351};
DE AltName: Full=NDH-1 subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
GN Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351,
GN ECO:0000313|EMBL:BAM31909.1};
GN ORFNames=HCBAA847_0670 {ECO:0000313|EMBL:BAM31909.1}, HCCG_01009
GN {ECO:0000313|EMBL:EFR46462.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31909.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:EFR46462.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 18818 {ECO:0000313|EMBL:EFR46462.1};
RG The Broad Institute Genome Sequencing Platform;
RA Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Helicobacter cinaedi strain CCUG 18818.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAM31909.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31909.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
RN [3] {ECO:0000313|EMBL:BAM31909.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31909.1};
RA Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000005755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 18818 {ECO:0000313|Proteomes:UP000005755};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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 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|HAMAP-Rule:MF_01351}.
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DR EMBL; AP012492; BAM31909.1; -; Genomic_DNA.
DR EMBL; DS990392; EFR46462.1; -; Genomic_DNA.
DR RefSeq; WP_002956320.1; NZ_DS990392.1.
DR AlphaFoldDB; I7HEM8; -.
DR GeneID; 66539117; -.
DR KEGG; hcb:HCBAA847_0670; -.
DR PATRIC; fig|1206745.3.peg.698; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_1_7; -.
DR OrthoDB; 9808559at2; -.
DR Proteomes; UP000005755; Unassembled WGS sequence.
DR Proteomes; UP000006036; Chromosome 1.
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:SF37; NADH-QUINONE OXIDOREDUCTASE SUBUNIT I 2; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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:BAM31909.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}.
FT DOMAIN 74..103
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 113..142
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 194..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
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 86
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 89
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 93
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 122
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 125
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 128
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 132
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 234 AA; 26192 MW; B54E8C66E97F8759 CRC64;
MKTEYRILPP RNKREKQLFL SRVALTFKTS FSLDLLSGLK TALGAFFSPN VTVQYPLESN
PLSPRYRAIH KLQRLLESEN ERCIGCGLCE KICTSNCIRI ITDRGEDGRK KILDYSINFG
RCIYCGLCAE VCPELAIIHG KGFENASVQR AHFGFKPELL ESQSSLIEYG GFGSVSYNAD
ERMIKTPLSY VLDSTKQEST QDSQNTQQAL QDSTKPSDTQ SATNDNNPKE SANV
//
