ID Q87NG8_VIBPA Unreviewed; 414 AA.
AC Q87NG8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE SubName: Full=Aspartate aminotransferase;
GN OrderedLocusNames=VP1900;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase 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; BA000031; BAC60163.1; -; Genomic_DNA.
DR RefSeq; NP_798279.2; NC_004603.1.
DR HSSP; P00509; 1ART.
DR ProteinModelPortal; Q87NG8; -.
DR STRING; 223926.VP1900; -.
DR EnsemblBacteria; BAC60163; BAC60163; BAC60163.
DR GeneID; 1189407; -.
DR KEGG; vpa:VP1900; -.
DR PATRIC; 20141960; VBIVibPar50997_1815.
DR HOGENOM; HOG000185899; -.
DR KO; K00832; -.
DR OMA; EFAIYIV; -.
DR ProtClustDB; PRK09257; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
SQ SEQUENCE 414 AA; 45478 MW; 37CF8B4B650AE523 CRC64;
MLKGINTSRP LRLTWMKIMF EKVVAAPADP ILGLTEEFKK DPRAEKINLG VGIYKNEQGE
TPVLATVKKA EAALIETEKT KSYLTIEGTA EYGLAVQKLL FGADAEIVAE KRAKTAQAPG
GTGALRVAGE FIKRQLGNVK IWISNPTWAN HNGVFTAAGL ETAQYTYYNA ETKDKDFDAM
LNDLQAASEG DIVLLHGCCH NPTGIDPTAE EWETLAKLIA EKKLLPLFDF AYQGFAKGVE
EDAAGLRIFA KYNKEILVAS SFSKNFGLYN ERVGAFTLVA ESEEVATTAF SQVKAIIRSI
YSNPPAHGSA VVTHILNNKE LRAEWEAEVQ EMRDRIQEMR ELFVATLKEE GVDADFSFIE
RQNGMFSFSG LSKEQVNRLK DEFAIYIVGS GRISVAGMTK SNMGPLCKGI AAVL
//