NUOH_BURCJ
ID NUOH_BURCJ Reviewed; 355 AA.
AC B4E5L5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=BceJ2315_22970; ORFNames=BCAL2337;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR52638.1; -; Genomic_DNA.
DR RefSeq; WP_006484885.1; NC_011000.1.
DR AlphaFoldDB; B4E5L5; -.
DR SMR; B4E5L5; -.
DR STRING; 216591.BCAL2337; -.
DR EnsemblBacteria; CAR52638; CAR52638; BCAL2337.
DR GeneID; 56558834; -.
DR KEGG; bcj:BCAL2337; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_4; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR BioCyc; BCEN216591:G1G1V-2580-MON; -.
DR Proteomes; UP000001035; Chromosome 1.
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..355
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_1000143580"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 355 AA; 39227 MW; 1B1F90C92FFBDDF0 CRC64;
MSLFDTINAG GAQLLGFAWP TVWAVVRILV VSVVILLCVA YLILWERKLI GWMHVRLGPN
RVGPGGLLQP IADVLKLLLK EVIQPTAASR WLYLIAPIMT VVPAFAVWAV IPFQAEAVLA
NVNAGLLYAM AISSIGVYAV ILAGWASNSK YAFLGAMRAA AQMVSYEISM GFALVLVLMT
AGSLNLSEIV GSQQHGFFAG HGVNFLSWNW LPLLPAFVVY FISGIAETNR HPFDVVEGES
EIVAGHMIDY SGMAFALFFL AEYINMIVIS ALAATLFLGG WDAPFEFLSF IPGIFWLVLK
VFALLSVFIW VRATFPRFRY DQIMRLGWKV FLPVTVIWVV VVGCWMMSPL NIWVK
