NUOH_XYLFT
ID NUOH_XYLFT Reviewed; 363 AA.
AC Q87EP8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 98.
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}; Synonyms=nqo8;
GN OrderedLocusNames=PD_0255;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO28141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009442; AAO28141.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012382440.1; NC_004556.1.
DR AlphaFoldDB; Q87EP8; -.
DR SMR; Q87EP8; -.
DR EnsemblBacteria; AAO28141; AAO28141; PD_0255.
DR GeneID; 58015811; -.
DR KEGG; xft:PD_0255; -.
DR HOGENOM; CLU_015134_0_1_6; -.
DR OMA; MYVGMGI; -.
DR Proteomes; UP000002516; 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; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Ubiquinone.
FT CHAIN 1..363
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000244967"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 166..186
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 239..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 363 AA; 40524 MW; ACD0C059D3B9B6B8 CRC64;
MNTWFLNVVD PLHQWFLGFG DIGVVLWTVL KILMIAIPLI VSVAFYVVWE RKLIGWMHVR
HGPMYVGMGL FQAFADVFKL LFKEVLYPSK AHKAIFVIAP LLTLAPSFAA WAVVPFDTKL
VLSNANVGLL YLLAMTSLGV YGIILAGWAS NSKYAFLGAM RSAAQVVSYE IAMGFALVGV
MIAAGSLNLS QIVMAQAGSS GFFDWFLIPL FPLFIVYWVS GVAETNRSPF DVVEGESEIV
AGHMVEYSGS VFALFFLAEY ANMILVSFLI SIFFLGGWLS PIQGWVSGQV SPLIDWVWNG
GWPWLLLKVL FFASAYIWFR ASFPRYRYDQ IMRLGWKVFI PLTIVWIAVT ALMVFSGVIQ
KGV
