(data stored in SCRATCH zone)

SWISSPROT: Q6FK92_CANGA

ID   Q6FK92_CANGA            Unreviewed;       371 AA.
AC   Q6FK92;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 89.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   Name=BAT2 {ECO:0000313|CGD:CAL0137043};
GN   OrderedLocusNames=CAGL0M00176g {ECO:0000313|CGD:CAL0137043,
GN   ECO:0000313|EMBL:CAG62328.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62328.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate = (S)-3-methyl-
CC       2-oxopentanoate + L-glutamate. {ECO:0000256|RuleBase:RU004517}.
CC   -!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2-
CC       oxopentanoate + L-glutamate. {ECO:0000256|RuleBase:RU004517}.
CC   -!- CATALYTIC ACTIVITY: L-valine + 2-oxoglutarate = 3-methyl-2-
CC       oxobutanoate + L-glutamate. {ECO:0000256|RuleBase:RU004517}.
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}.
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DR   EMBL; CR380959; CAG62328.1; -; Genomic_DNA.
DR   RefSeq; XP_449352.1; XM_449352.1.
DR   ProteinModelPortal; Q6FK92; -.
DR   STRING; 284593.XP_449352.1; -.
DR   PRIDE; Q6FK92; -.
DR   EnsemblFungi; CAG62328; CAG62328; CAGL0M00176g.
DR   KEGG; cgr:CAGL0M00176g; -.
DR   CGD; CAL0137043; BAT2.
DR   EuPathDB; FungiDB:CAGL0M00176g; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276704; -.
DR   InParanoid; Q6FK92; -.
DR   KO; K00826; -.
DR   OMA; LTACNIF; -.
DR   OrthoDB; EOG092C2KT2; -.
DR   Proteomes; UP000002428; Chromosome M.
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:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR033939; BCAT_family.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK92.
DR   SWISS-2DPAGE; Q6FK92.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|RuleBase:RU004517};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU004517};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transferase {ECO:0000256|RuleBase:RU004517}.
FT   MOD_RES     197    197       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR006468-1}.
SQ   SEQUENCE   371 AA;  41577 MW;  31440A536670222C CRC64;
     MDASRLKITK VSTPSERKPN DQLVFGKTFT DHMLTIEWTS ENGWDAPEIK PYGKLCLDPS
     SIVFHYAFEL FEGMKAYRTK DGKIAMFRPE KNMERMNKSA ARICLPTFDG EELIKLIGKL
     IELDKHLIPE GEGYSLYIRP TLIGTSEGLG VKEPDRALLF VICSPVGPYY KTGFKAVRLD
     ATDYATRAWP GGVGDKKLGA NYAPCVLPQT QAAAKGFQQN LWLFGPEHYV TEVGTMNAFF
     AFNCKETGKK ELVTAPLDGT ILEGVTRDSI LTLARKYLDP NEWEINERYF TIHEVQEKAH
     KGELLEAFGS GTAAIVSPIK EIGWKDTIIN VPLIPGEQSG PLTKQIASWM MDIQYGKVEL
     DNWLRIVADI N
//

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