ID A0A1L8CPM5_9PROT Unreviewed; 123 AA.
AC A0A1L8CPM5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=MMIC_P1809 {ECO:0000313|EMBL:GAV20834.1};
OS Mariprofundus micogutta.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921010 {ECO:0000313|EMBL:GAV20834.1, ECO:0000313|Proteomes:UP000231632};
RN [1] {ECO:0000313|EMBL:GAV20834.1, ECO:0000313|Proteomes:UP000231632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ET2 {ECO:0000313|EMBL:GAV20834.1,
RC ECO:0000313|Proteomes:UP000231632};
RX PubMed=27766355; DOI=10.1007/s00203-016-1307-4;
RA Makita H., Tanaka E., Mitsunobu S., Miyazaki M., Nunoura T., Uematsu K.,
RA Takaki Y., Nishi S., Shimamura S., Takai K.;
RT "Mariprofundus micogutta sp. nov., a novel iron-oxidizing
RT zetaproteobacterium isolated from a deep-sea hydrothermal field at the
RT Bayonnaise knoll of the Izu-Ogasawara arc, and a description of
RT Mariprofundales ord. nov. and Zetaproteobacteria classis nov.";
RL Arch. Microbiol. 199:335-346(2017).
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 membrane {ECO:0000256|HAMAP-Rule:MF_01394,
CC ECO:0000256|RuleBase:RU003639}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_01394, 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}.
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:GAV20834.1}.
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DR EMBL; BDFD01000016; GAV20834.1; -; Genomic_DNA.
DR RefSeq; WP_072660135.1; NZ_BDFD01000016.1.
DR AlphaFoldDB; A0A1L8CPM5; -.
DR STRING; 1921010.MMIC_P1809; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000231632; Unassembled WGS sequence.
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; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR PANTHER; PTHR11058:SF9; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
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:GAV20834.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 65..86
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ SEQUENCE 123 AA; 13885 MW; 114C4E50AABC9B63 CRC64;
MGATYLANEY APIFIFILIA IGMGAAPLVL TALLAEQKPD AEKLSAYECG FEAFEDARLQ
FDVRFYLLAI LFVIFDLESA FLFPWAIVLD QIGLFGFVEM VLFLVILLVG YIYAWKKGAL
QWE
//
