(data stored in ACNUC7421 zone)

SWISSPROT: Q13IV1_PARXL

ID   Q13IV1_PARXL            Unreviewed;       465 AA.
AC   Q13IV1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABE35988.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ABE35988.1};
GN   ORFNames=Bxe_C0061 {ECO:0000313|EMBL:ABE35988.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35988.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35988.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35988.1,
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; ABE35988.1; -; Genomic_DNA.
DR   RefSeq; WP_011493248.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0061; -.
DR   EnsemblBacteria; ABE35988; ABE35988; Bxe_C0061.
DR   GeneID; 4009608; -.
DR   KEGG; bxb:DR64_8364; -.
DR   KEGG; bxe:Bxe_C0061; -.
DR   PATRIC; fig|266265.5.peg.7840; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   KO; K15785; -.
DR   OMA; SGHPICA; -.
DR   OrthoDB; 478143at2; -.
DR   BioCyc; BXEN266265:BXE_RS37060-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; Q13IV1.
DR   SWISS-2DPAGE; Q13IV1.
KW   Aminotransferase {ECO:0000313|EMBL:ABE35988.1};
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:ABE35988.1}.
SQ   SEQUENCE   465 AA;  50161 MW;  43403E282B98E412 CRC64;
     MTQLDQLFDA DRAHFMHPST HAHDHASGAL PGRIVTGAQG IRIEDHQGKS YIDAFAGLYC
     VNIGYGRTEV AEAIYEQAKK LAYYHTYVGH STDTIIELSS RIIEWAPQGM KKVYYGMSGS
     DANETQIKLV WYYNNVKGRP DKKKIISRQR GYHGSGIVTG SLTGLASFHQ YFDLPIGRVK
     HTVCPHWYRH APAGMNEAQF VAYCVEELEK LIAQEGADTI AAFIAEPVMG TGGILPPPAG
     YWPAIQQVLK KHDILLICDE VVCGFGRLGS KMGAQHYGIA PDLITVAKGL TSAYAPLSGV
     IVSEGVWDVI DKASQEFGAM GHGWTYSGHP ICAAAALANL DILERENLTQ NAAQTGAYLL
     EQLHAAFDSH PLVGEVRGAG MLAALEFMAD KDGRQPFDAA LKVGPRVSAA ALQRGLIARA
     MPHGDILGFA PPLITSRSEV DEIVKLAREA VDEVASAVLS PAASA
//

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