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Database: UniProt/TrEMBL
Entry: Q87NG8_VIBPA
LinkDB: Q87NG8_VIBPA
Original site: Q87NG8_VIBPA 
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.
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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
//
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