(data stored in ACNUC7421 zone)

SWISSPROT: Q13H40_PARXL

ID   Q13H40_PARXL            Unreviewed;       466 AA.
AC   Q13H40;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABE36599.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ABE36599.1};
GN   ORFNames=Bxe_C0784 {ECO:0000313|EMBL:ABE36599.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36599.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36599.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36599.1,
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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000272; ABE36599.1; -; Genomic_DNA.
DR   RefSeq; WP_011493855.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0784; -.
DR   EnsemblBacteria; ABE36599; ABE36599; Bxe_C0784.
DR   GeneID; 4010215; -.
DR   KEGG; bxb:DR64_7738; -.
DR   KEGG; bxe:Bxe_C0784; -.
DR   PATRIC; fig|266265.5.peg.8466; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   OMA; WLPLMGT; -.
DR   OrthoDB; 478143at2; -.
DR   BioCyc; BXEN266265:BXE_RS40015-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13H40.
DR   SWISS-2DPAGE; Q13H40.
KW   Aminotransferase {ECO:0000313|EMBL:ABE36599.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000313|EMBL:ABE36599.1}.
SQ   SEQUENCE   466 AA;  49868 MW;  366AB5C26D153762 CRC64;
     MSKTSLIAAD RKHLIHPVIN YRAHEARGAT VLESGQGAYL RDIDGNELLD AFSGLWCVNV
     GYGQQSIVEA ATRQMTKLPY ATTYFHFSSE PAIELADKLV ALAPASLQHV YFTLGGSDAV
     DSAIRFITHY FNATGRPSKK QMIALERGYH GSSSVGAGLT ALPAFHRNFD LPLPHQHHLP
     SPYAYRQTHG DDAQALIAAS VAALEAKVAA LGTDNVAAFF CEPIQGSGGV IVPPVGWLKA
     MRDACRRLDI LFVADEVITG FGRTGPLFAC EAEQVEPDLM TVAKGLTSGY APMGAVLMSD
     EIYQGIAGDA RDTAIVGHGQ TYSAHPVSAA IGLEVLRLYQ EGGLLANGQA QAPRFAAGLD
     ALLGHPLVGD SRHRGLLGAL ELVADKDSRA RFDPALKLPD RIAAAAYRNR LVFRAFGDSI
     LGFAPALCFG EAEFEQMFGR LKRTLDEVLD ETEVRAALRT AGRAAA
//

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