ID A7GW70_CAMC5 Unreviewed; 129 AA.
AC A7GW70;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394};
GN Name=nuoA {ECO:0000256|HAMAP-Rule:MF_01394,
GN ECO:0000313|EMBL:EAU00592.1};
GN ORFNames=CCV52592_1529 {ECO:0000313|EMBL:EAU00592.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU00592.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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_01394}.
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_01394,
CC ECO:0000256|RuleBase:RU003639};
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_01394}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01394}. Cell membrane {ECO:0000256|RuleBase:RU003639}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003639}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000256|ARBA:ARBA00008472, ECO:0000256|HAMAP-Rule:MF_01394,
CC ECO:0000256|RuleBase:RU003639}.
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DR EMBL; CP000767; EAU00592.1; -; Genomic_DNA.
DR RefSeq; WP_009649869.1; NC_009715.2.
DR AlphaFoldDB; A7GW70; -.
DR STRING; 360105.CCV52592_1529; -.
DR KEGG; ccv:CCV52592_1529; -.
DR HOGENOM; CLU_119549_0_2_7; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000006380; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058:SF22; NADH-QUINONE OXIDOREDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR11058; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW Oxidoreductase {ECO:0000313|EMBL:EAU00592.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01394};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01394}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ SEQUENCE 129 AA; 14943 MW; 6C429B4F11883406 CRC64;
MSHSQLASPY LGAFMILVLA TCSFVLITFL SSRIGKKLAN RNTERLKSSI YECGPEVVKQ
PNKINIHYFF YAILFILFDV EVIFMYPWAV DFRLLGAFGL IEMLLFVTLL LIGFIYAWRK
GVFEWQSIK
//
