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NUOH_DEHM1
ID   NUOH_DEHM1              Reviewed;         353 AA.
AC   Q3Z7Z7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=DET0927;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(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 membrane {ECO:0000255|HAMAP-Rule:MF_01350};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000027; AAW39808.1; -; Genomic_DNA.
DR   RefSeq; WP_010936631.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z7Z7; -.
DR   SMR; Q3Z7Z7; -.
DR   STRING; 243164.DET0927; -.
DR   EnsemblBacteria; AAW39808; AAW39808; DET0927.
DR   KEGG; det:DET0927; -.
DR   PATRIC; fig|243164.10.peg.877; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_0; -.
DR   OMA; MYVGMGI; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000008289; 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.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN           1..353
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000240069"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        229..249
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"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   353 AA;  39155 MW;  8113A2139CEE5E61 CRC64;
     MSDFWVHLLV YLVILFGFVI VSVLLFIWLE RRFIGRFQLR PGPNRAGPFG LLQPIADAIK
     VLIKEDIIPT ESDKGVFWLA PLVAFVPVML MFAAIPFADG AMLVDLNIGI LYILAVSSVT
     VIGIFMAGWS SNSKYSLLGA MRTIAQEVSY EIPLVLSILG VVMLTGSLSM NEIVKAQSVP
     FVLLQPLGFF VYLSAAMAEI NRTPFDLLEA ESEIIAGFHT EYSGMKFGLF YLMEYAEVLA
     ISAIATTLFL GGWQGPLLHP VIWFITKVLI IFMFIIWVRA TIPRLRIDQV MAFGWKFLLP
     LSLANLVITA FEILAAPDMN TAVLIGINIA VMFGLILLFS RFYKLGGGRV SVK
 
 
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