(data stored in SCRATCH zone)

SWISSPROT: C5BBA4_EDWI9

ID   C5BBA4_EDWI9            Unreviewed;       309 AA.
AC   C5BBA4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   SubName: Full=Branched-chain amino acid aminotransferase, putative {ECO:0000313|EMBL:ACR67339.1};
DE            EC=2.6.1.42 {ECO:0000313|EMBL:ACR67339.1};
GN   OrderedLocusNames=NT01EI_0079 {ECO:0000313|EMBL:ACR67339.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67339.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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; CP001600; ACR67339.1; -; Genomic_DNA.
DR   RefSeq; WP_015869560.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0079; -.
DR   EnsemblBacteria; ACR67339; ACR67339; NT01EI_0079.
DR   GeneID; 7959798; -.
DR   KEGG; eic:NT01EI_0079; -.
DR   PATRIC; fig|634503.3.peg.72; -.
DR   eggNOG; ENOG4105CM2; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276706; -.
DR   KO; K00826; -.
DR   OMA; NFFGITH; -.
DR   OrthoDB; POG091H02UL; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR005785; B_amino_transI.
DR   InterPro; IPR033939; BCAT_family.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01122; ilvE_I; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BBA4.
DR   SWISS-2DPAGE; C5BBA4.
KW   Aminotransferase {ECO:0000313|EMBL:ACR67339.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000313|EMBL:ACR67339.1}.
SQ   SEQUENCE   309 AA;  33932 MW;  328C03A4C57EB3B2 CRC64;
     MTTKKADYIW FNGDMVPWGE ARVHVMSHAL HYGTSVFEGV RCYETHRGPA VFRHREHMQR
     LHDSARIYRM PLAYSVEELM AACRETLRRN QLSSAYIRPL VFIGDVGMGV NPPAGYGTDV
     ILAAFPWGAY LGEEALEQGI DAMVSSWHRA APNTIPTAAK AGGNYLSSLL VGSEARRHGY
     QEGIALDVHG YVSEGAGENL FMVKNGVIFT PPFTSAALPG ITRDAIITLA QAQGLEVREQ
     VLSREALYLA DEIFMSGTAA EITPVRSVDG IQVGIGRCGP ITKRVQQAFF GLFNGQTEDR
     FGWLDPVNP
//

If you have problems or comments...

PBIL Back to PBIL home page