(data stored in ACNUC7421 zone)

SWISSPROT: Q145J6_PARXL

ID   Q145J6_PARXL            Unreviewed;       484 AA.
AC   Q145J6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
DE            EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000204};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
GN   ORFNames=Bxe_A4006 {ECO:0000313|EMBL:ABE28993.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28993.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28993.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28993.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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. {ECO:0000256|PIRNR:PIRNR000204}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC         Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349;
CC         EC=7.1.1.1; Evidence={ECO:0000256|PIRNR:PIRNR000204};
CC   -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC       {ECO:0000256|PIRNR:PIRNR000204}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000270; ABE28993.1; -; Genomic_DNA.
DR   RefSeq; WP_011486817.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4006; -.
DR   EnsemblBacteria; ABE28993; ABE28993; Bxe_A4006.
DR   GeneID; 4003401; -.
DR   KEGG; bxb:DR64_1683; -.
DR   KEGG; bxe:Bxe_A4006; -.
DR   PATRIC; fig|266265.5.peg.481; -.
DR   eggNOG; ENOG4105C15; Bacteria.
DR   eggNOG; COG1282; LUCA.
DR   HOGENOM; HOG000243958; -.
DR   KO; K00325; -.
DR   OMA; GESIREN; -.
DR   OrthoDB; 788546at2; -.
DR   BioCyc; BXEN266265:BXE_RS02280-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012136; NADH_DH_b.
DR   InterPro; IPR034300; PNTB-like.
DR   Pfam; PF02233; PNTB; 1.
DR   PIRSF; PIRSF000204; PNTB; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145J6.
DR   SWISS-2DPAGE; Q145J6.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR000204};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000204};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000204, ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|PIRNR:PIRNR000204};
KW   NADP {ECO:0000256|PIRNR:PIRNR000204};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE28993.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Translocase {ECO:0000256|PIRNR:PIRNR000204};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     24       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     36     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     65     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     96    116       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    143    164       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    204       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    210    228       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    235    253       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    279       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        7    481       PNTB. {ECO:0000259|Pfam:PF02233}.
SQ   SEQUENCE   484 AA;  50535 MW;  020470D6C96E242B CRC64;
     MSLNVVTLLY LVASVCFIQA LKGLSNPKTA RIGNTFGMAG MAIAILTTIA LIVKQANGLG
     SNLGLGLGLL LVALVIGGAI GAFVAARVEM TKMPELVAAM HSLIGLAAVC IAYAVVSEPA
     AFGLVDPENT APGFLPYGNR VELFIGTFVG AITFSGSVIA FGKLSGKYKF RLFQGAPVVY
     AGQHLINLLL ALAMLGFGVI FFLTQSWLPF IIMTVIAFVL GVLIIIPIGG ADMPVVVSML
     NSYSGWAAAG IGFSLNNPML IIAGSLVGSS GAILSYIMCR AMNRSFFNVI LGGFGNEPGA
     AAAGGAAEQR PVKSGSADDA AFMLGNAETV VIVPGYGLAV ARAQHALKEL TDKLVGKGIE
     VKYAIHPVAG RMPGHMNVLL AEAEVPYDMV YEMDDINGEF GQVDVVLVLG ANDVVNPAAK
     NDPKSPIAGM PIIEAYKART VIVNKRSMAA GYAGLDNDLF YMDKTMMVFG DAKKVIEDMV
     KAVE
//

If you have problems or comments...

PBIL Back to PBIL home page