ID NUOH_SALA4 Reviewed; 325 AA.
AC B5EZK3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=NADH-quinone oxidoreductase subunit H;
DE EC=1.6.99.5;
DE AltName: Full=NADH dehydrogenase I subunit H;
DE AltName: Full=NDH-1 subunit H;
GN Name=nuoH; OrderedLocusNames=SeAg_B2461;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RA Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M.,
RA Leclerc J., Cebula T., Sebastian Y.;
RT "Complete genome of Salmonella agona strain SL483.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is
CC believed to be ubiquinone. Couples the redox reaction to proton
CC translocation (for every two electrons transferred, four hydrogen
CC ions are translocated across the cytoplasmic membrane), and thus
CC conserves the redox energy in a proton gradient. This subunit may
CC bind ubiquinone (By similarity).
CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC complex (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (Potential).
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
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DR EMBL; CP001138; ACH52925.1; -; Genomic_DNA.
DR RefSeq; YP_002147280.1; NC_011149.1.
DR STRING; 454166.SeAg_B2461; -.
DR PRIDE; B5EZK3; -.
DR EnsemblBacteria; ACH52925; ACH52925; SeAg_B2461.
DR GeneID; 6795705; -.
DR KEGG; sea:SeAg_B2461; -.
DR PATRIC; 18483206; VBISalEnt65316_2409.
DR eggNOG; COG1005; -.
DR HOGENOM; HOG000228276; -.
DR KO; K00337; -.
DR OMA; VGEYINI; -.
DR ProtClustDB; PRK06076; -.
DR BioCyc; SENT454166:GHBA-4627-MONOMER; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:EC.
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; Complete proteome; Membrane; NAD;
KW Oxidoreductase; Quinone; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1 325 NADH-quinone oxidoreductase subunit H.
FT /FTId=PRO_1000143617.
FT TRANSMEM 11 31 Helical; (Potential).
FT TRANSMEM 50 69 Helical; (Potential).
FT TRANSMEM 81 101 Helical; (Potential).
FT TRANSMEM 114 134 Helical; (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TRANSMEM 186 206 Helical; (Potential).
FT TRANSMEM 237 257 Helical; (Potential).
FT TRANSMEM 265 285 Helical; (Potential).
FT TRANSMEM 304 324 Helical; (Potential).
SQ SEQUENCE 325 AA; 36292 MW; 85A7F3A941EA873D CRC64;
MSWITPDLIE ILLSILKAVV ILLVVVTCGA FMSFGERRLL GLFQNRYGPN RVGWGGSLQL
VADMIKMFFK EDWIPKFSDR VIFTLAPMIA FTSLLLSFAI VPVSPNWVVA DLNIGILFFL
MMAGLAVYAV LFAGWSSNNK YSLLGAMRAS AQTVSYEVFL GLSLMGVVAQ AGSFNMTDIV
NNQAHLWNVI PQFFGFVTFA IAGVAVCHRH PFDQPEAEQE LADGYHIEYS GMKFGLFFVG
EYIGIVTVSA LMVTLFFGGW HGPFLPPFVW FALKTAFFMM MFILIRASLP RPRYDQVMSF
GWKVCLPLTL INLLVTAAVI LWQAQ
//