ID   NUOH_AROAE              Reviewed;         349 AA.
AC   Q5P1E3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH dehydrogenase I subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=nuoH {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=AZOSEA27460;
GN   ORFNames=ebA4842;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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. This subunit may bind ubiquinone.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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_01350};
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:0000255|HAMAP-Rule:MF_01350}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01350}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR   EMBL; CR555306; CAI08871.1; -; Genomic_DNA.
DR   RefSeq; WP_011238554.1; NC_006513.1.
DR   AlphaFoldDB; Q5P1E3; -.
DR   SMR; Q5P1E3; -.
DR   STRING; 76114.ebA4842; -.
DR   EnsemblBacteria; CAI08871; CAI08871; ebA4842.
DR   KEGG; eba:ebA4842; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_4; -.
DR   OMA; WSGWASN; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000006552; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..349
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000244889"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   349 AA;  38454 MW;  1CC19C19482C735B CRC64;
     MEALLEPVVQ LFGPAWPAVW TLTKIVAIIA PLMLCVAYLT LAERKVIGYM QVRIGPNRVG
     PKGLLQPIAD GMKLLFKEII VPTGASKGLF ILGPILAIAP SLAAWAVVPF GEGMVLADVN
     AGLLFLLAIT SVEVYGVIIA GWASNSKYPF LGSMRAAAQM VSYEVAMGFA LICVLLISAS
     LNLTDIVRSQ GQGQFHEMGL SFLSWNWIPL FPMFIVFLIS GIAETNRAPF DVVEGESEVV
     AGHMVEYSGM AFALFFLAEY ANMILVSILT SVLFVGGWLS PVSFLPDGFF WLALKTAFFL
     FVFLWARATF PRFRYDHIMR LGWKVFIPIT LVWVIVVAVW MMSPLSIWK