ID   A1T1C0_MYCVP            Unreviewed;       479 AA.
AC   A1T1C0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   01-MAY-2013, entry version 47.
DE   RecName: Full=NAD(P) transhydrogenase subunit beta;
DE            EC=1.6.1.2;
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta;
DE   Flags: Precursor;
GN   OrderedLocusNames=Mvan_0119;
OS   Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled
CC       to respiration and ATP hydrolysis and functions as a proton pump
CC       across the membrane (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
CC   -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000511; ABM10970.1; -; Genomic_DNA.
DR   RefSeq; YP_950976.1; NC_008726.1.
DR   ProteinModelPortal; A1T1C0; -.
DR   SMR; A1T1C0; 307-473.
DR   STRING; 350058.Mvan_0119; -.
DR   EnsemblBacteria; ABM10970; ABM10970; Mvan_0119.
DR   GeneID; 4648051; -.
DR   KEGG; mva:Mvan_0119; -.
DR   PATRIC; 18178370; VBIMycVan31953_0121.
DR   eggNOG; COG1282; -.
DR   HOGENOM; HOG000243958; -.
DR   KO; K00325; -.
DR   OMA; GNVGWII; -.
DR   ProtClustDB; CLSK636520; -.
DR   BioCyc; MVAN350058:GIWR-122-MONOMER; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   InterPro; IPR012136; NADH_DH_b.
DR   Pfam; PF02233; PNTB; 1.
DR   PIRSF; PIRSF000204; PNTB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   NADP; Oxidoreductase; Signal.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    479       Potential.
FT                                /FTId=PRO_5000207038.
SQ   SEQUENCE   479 AA;  49826 MW;  EFE18F0770A52F6F CRC64;
     MFTLETAATA AYVVAALLFI LALAGLSRHE TSRAGNTFGI VGMVVALVAT IALALARHIE
     PLGLALLVGA MTIGAAIGLW RAKIVEMTGM PELIALLHSF VGLAAVLVGW NGYLHVEGDP
     GSAEALQLGS EGMLGIHSAE VVIGVFIGAV TFTGSIVANL KLSARIKSAP LMLPGKNILN
     VGALVVFIAL TVWFVIDPQL WLLVVVTVLA LALGWHLVAS IGGGDMPVVV SMLNSYSGWA
     AAAAGFLLGN DLLIVTGALV GSSGAYLSYI MCKAMNRSFI SVIAGGFGIE AGPAEDKDYG
     EHREITAEGA AELLASASSV IITPGYGMAV AQAQYGVADL TRKLRDRGVD VRFGIHPVAG
     RLPGHMNVLL AEAKVPYDIV LEMDEINDDF DGTSVVLVIG ANDTVNPAAS EDPGSPIAGM
     PVLTVWNADN VIVFKRSMAS GYAGVQNPLF FRENTQMLFG DAKDRVDAIN AALSVAEHV
//