(data stored in ACNUC7421 zone)

SWISSPROT: Q13HL3_PARXL

ID   Q13HL3_PARXL            Unreviewed;       483 AA.
AC   Q13HL3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
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_C0526 {ECO:0000313|EMBL:ABE36426.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36426.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36426.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36426.1,
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; CP000272; ABE36426.1; -; Genomic_DNA.
DR   RefSeq; WP_011493682.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0526; -.
DR   EnsemblBacteria; ABE36426; ABE36426; Bxe_C0526.
DR   GeneID; 4010040; -.
DR   KEGG; bxb:DR64_7921; -.
DR   KEGG; bxe:Bxe_C0526; -.
DR   PATRIC; fig|266265.5.peg.8286; -.
DR   eggNOG; ENOG4105C15; Bacteria.
DR   eggNOG; COG1282; LUCA.
DR   HOGENOM; HOG000243958; -.
DR   KO; K00325; -.
DR   OMA; DNCRMLY; -.
DR   OrthoDB; 788546at2; -.
DR   BioCyc; BXEN266265:BXE_RS39150-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
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; Q13HL3.
DR   SWISS-2DPAGE; Q13HL3.
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:ABE36426.1};
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     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     57       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     69     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    121       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    133    153       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    174    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    222       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    229    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    254    273       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       13    472       PNTB. {ECO:0000259|Pfam:PF02233}.
SQ   SEQUENCE   483 AA;  49592 MW;  2706D7C3B863F8F2 CRC64;
     MLTLLPQLGI GIADLAAAFL FLYGLHRMSS PVTAPSGIFV AGIGMAVAVL ASFLYAFGVD
     AAARPDLPVN LVLALVALAI GGGVAWWGGR KVAMTAMPQM VAIYNGMGGG AAGAIAAVEL
     FGNKARGVTE LVATLAGAFI GAVSLSGSLI AWAKLDGVIN KPVRVKGQQV FNGLVLLATV
     AVGACIVVAS LDQRALILAM PAWIYVFFGC ALAVGILMTL PIGGADMPVV ISIFNAFTGL
     AVGIEGYVLQ NPALMIAGMV VGAAGMLLTL LMAKAMNRSV SNVVFTNFGE VASRKQGKIK
     GSLKPVQPGD AGIAMRYAAS VIIVPGYGLA VSQGQGKLFE FVKLLQAGGV SVKFAVHPVA
     GRMPGQMDVL LAEAGVPYDM IFQLEDINEQ FASTDVALVI GANDVVNPAA RTDKSSVIFG
     MPILDADKAK QVFVIKRGEG NGYAGIVNAL FYADTCSMVY GDAQGVLVKM IEAVRGLGLP
     AVA
//

If you have problems or comments...

PBIL Back to PBIL home page