ID NUOH_FRAT1 Reviewed; 336 AA.
AC Q14K31;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 01-MAY-2013, entry version 57.
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=FTF0038;
OS Francisella tularensis subsp. tularensis (strain FSC 198).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC 198;
RX PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT "Genome sequencing shows that European isolates of Francisella
RT tularensis subspecies tularensis are almost identical to US laboratory
RT strain Schu S4.";
RL PLoS ONE 2:E352-E352(2007).
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 14 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; AM286280; CAL08054.1; -; Genomic_DNA.
DR RefSeq; YP_666245.1; NC_008245.1.
DR STRING; 393115.FTF0038; -.
DR EnsemblBacteria; CAL08054; CAL08054; FTF0038.
DR GeneID; 4200747; -.
DR KEGG; ftf:FTF0038; -.
DR PATRIC; 17958692; VBIFraTul133500_0041.
DR eggNOG; COG1005; -.
DR HOGENOM; HOG000228276; -.
DR KO; K00337; -.
DR OMA; AEYVNMV; -.
DR ProtClustDB; CLSK934342; -.
DR BioCyc; FTUL393115:GJUT-38-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 1 336 NADH-quinone oxidoreductase subunit H.
FT /FTId=PRO_0000298814.
FT TRANSMEM 4 24 Helical; (Potential).
FT TRANSMEM 75 95 Helical; (Potential).
FT TRANSMEM 108 128 Helical; (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TRANSMEM 181 201 Helical; (Potential).
FT TRANSMEM 233 253 Helical; (Potential).
FT TRANSMEM 272 292 Helical; (Potential).
FT TRANSMEM 308 328 Helical; (Potential).
SQ SEQUENCE 336 AA; 37642 MW; 28F125A9F17D822D CRC64;
MLGYILWTSL YVLLIVIPLI LVVAYYTYAE RKVIGYMQDR IGPNRVGSFG LLQPIFDALK
LFLKEIIVPT NSNRYLFFIA PILAFAPAYA AWAVIPFSKG VVLSDMNLGL LYILAMTSFS
IYGIVIAGWA SNSKYSLFGA LRAGAQVISY ELAMGFAIVG VVIAAGSMGI TGIIEAQSGG
IWHWYFIPLF PLFIVYFIAG IAETNRAPFD VVEGESEIVA GHHIEYTGSR FALFFLAEYA
NMILISILTS IMFLGGWNSP FQATALESIF GFVPGVVWLF AKTGIFMFMF LWVRATYPRY
RYDQIMRLGW KIFIPLTFVW VVIVACMVRL GVGPWW
//
