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NUOH1_NITOC
ID   NUOH1_NITOC             Reviewed;         319 AA.
AC   Q3JC21;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=NADH-quinone oxidoreductase subunit H 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NDH-1 subunit H 1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=nuoH1 {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=Noc_1121;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/aem.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA57625.1; -; Genomic_DNA.
DR   RefSeq; WP_002811551.1; NC_007484.1.
DR   AlphaFoldDB; Q3JC21; -.
DR   SMR; Q3JC21; -.
DR   STRING; 323261.Noc_1121; -.
DR   EnsemblBacteria; ABA57625; ABA57625; Noc_1121.
DR   KEGG; noc:Noc_1121; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_6; -.
DR   OMA; FTWVERR; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000006838; 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..319
FT                   /note="NADH-quinone oxidoreductase subunit H 1"
FT                   /id="PRO_0000240090"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   319 AA;  35406 MW;  CA05220EF8EEBD17 CRC64;
     MNATLTSLFN IFGILGTLLT LAALLIWIER RLLGFWQERY GPNRVGPFGI LQVVADAIKL
     LTKEDWVPPF ADKLVFILAP TVVVIATLLA FAVIPFTPYI GIIDLNIGLL FFLAMSSLSV
     YSVVLGGWAS NNKYSLMGAL RAAAQMLSYE VFMGLSLMGV VMLAGTFNLR EIVAAQQDMW
     FCIPQFLGLV VFLIAGIAEA HRLPFDLPEA ETELIAGFHT EYSGMKFGLF FVGEYLAILL
     ISALIVTLFF GGWQGPWLPP LVWFFIKFSF FVLFFILLRA ALPRPRYDQL MAYGWKLMLP
     LALLNLVITG AVVLALDGT
 
 
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