ID   Q6FT63_CANGA            Unreviewed;       565 AA.
AC   Q6FT63;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   01-MAY-2013, entry version 59.
DE   SubName: Full=Strain CBS138 chromosome G complete sequence;
GN   OrderedLocusNames=CAGL0G05071g;
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   mitosporic Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; CR380953; CAG59508.1; -; Genomic_DNA.
DR   RefSeq; XP_446581.1; XM_446581.1.
DR   ProteinModelPortal; Q6FT63; -.
DR   GeneID; 2888433; -.
DR   KEGG; cgr:CAGL0G05071g; -.
DR   HOGENOM; HOG000206826; -.
DR   KO; K00654; -.
DR   OrthoDB; EOG4VT95J; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Pyridoxal phosphate.
SQ   SEQUENCE   565 AA;  63879 MW;  2B194E11479D73BF CRC64;
     MSTNGSTVSD YKYVPLIKHE PLSDEQQKEN EFGELTSDAY RFKVHSREGK PIRKPVIDTP
     PYYISLVTYL NYLILIILGH IHDFLGMRLQ RNKHLDILEH DGMAPWFSNF DSFFARRMKM
     RIDDCFSRPT TGVPGRFIRC ITRISHNLNE YFTYPGTTSM CLNLSSYNYL GFAQSKGQCT
     DAALESVDKY GIHTGGSRTQ IGTTDLHRLT EELVADFVGK EDAMVFSMGY GTNANFFNAF
     LDRKCLVISD ELNHTSIRTG VRLSGAAVRT FKHGDMEGLE KLIRDQIVLG QPKTNRPWKK
     ILICVEGLFS MEGTMCNLPE LIALKKKYKC YLFVDEAHSI GAIGPTGRGV CEYFGVNPHD
     VDILMGTFTK SFGAAGGYIA TDKWVMDRLR LDLTTTSYAE PTPAPVLAQI VSSLRTIKGD
     ICPGEGRERL ERIAFNSRYL RLALLRLGFI VYGIPDSPVI PMLLYCPSKM PAFSRMMLQR
     KIAVVVVAYP ATPLIESRVR FCMSASITKE DIDYLLRHVD EVGEKLNLKL NSGKSSIDGK
     APRWDIEEVI RRTPEDCKDD KYFVL
//