ID   GABAT_USTMA             Reviewed;         509 AA.
AC   P49604; A0A0D1E6G7; Q4PFN3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=4-aminobutyrate aminotransferase;
DE            EC=2.6.1.19;
DE   AltName: Full=GABA aminotransferase;
DE            Short=GABA-AT;
DE   AltName: Full=Gamma-amino-N-butyrate transaminase;
DE            Short=GABA transaminase;
GN   Name=GATA; ORFNames=UMAG_01080;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=518;
RX   PubMed=8598057; DOI=10.1007/bf02208617;
RA   Straffon M.J., Hynes M.J., Davis M.A.;
RT   "Characterization of the ugatA gene of Ustilago maydis, isolated by
RT   homology to the gatA gene of Aspergillus nidulans.";
RL   Curr. Genet. 29:360-369(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deaminates gamma-aminobutyric acid (GABA) to succinate-
CC       semialdehyde, which in turn is converted to succinate by the succinate
CC       semialdehyde dehydrogenase (By similarity). Not required for the
CC       utilization of GABA as nitrogen source. {ECO:0000250,
CC       ECO:0000269|PubMed:8598057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P17649};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O13837}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by GABA and beta-alanine. Is not subject to
CC       nitrogen catabolite repression. {ECO:0000269|PubMed:8598057}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U28655; AAA98560.1; -; Genomic_DNA.
DR   EMBL; CM003141; KIS71171.1; -; Genomic_DNA.
DR   PIR; S68116; S68116.
DR   RefSeq; XP_011387041.1; XM_011388739.1.
DR   AlphaFoldDB; P49604; -.
DR   SMR; P49604; -.
DR   STRING; 5270.UM01080P0; -.
DR   PRIDE; P49604; -.
DR   EnsemblFungi; KIS71171; KIS71171; UMAG_01080.
DR   GeneID; 23562197; -.
DR   KEGG; uma:UMAG_01080; -.
DR   VEuPathDB; FungiDB:UMAG_01080; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   InParanoid; P49604; -.
DR   OMA; DPPDMVT; -.
DR   OrthoDB; 566705at2759; -.
DR   Proteomes; UP000000561; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:EnsemblFungi.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..509
FT                   /note="4-aminobutyrate aminotransferase"
FT                   /id="PRO_0000120381"
FT   BINDING         166..167
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   BINDING         387
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   MOD_RES         363
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   CONFLICT        337
FT                   /note="G -> GT (in Ref. 1; AAA98560)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  55993 MW;  9ECAFAE83FE4DD4C CRC64;
     MISSKATSAA RACARTSRVM QQQQRRLLAT VVSSSSLFPG EPSSPHVVTS QIPGPKSKEL
     SDRIGTFQEN RTHGFVVDYA KSQGNWIADA DGNVLLDMFA QIASIAIGYN NPDLLALAKT
     DEFITATMNR AALGSFPPTN WQELVETSFG TVKPDGLNNI FTAMCGSCAN ENAFKASFMA
     YRARERGEKA EFTPEEMSSC MKNQSPGSPD LSILSFTSAF HGRLFGSLSA TRSKAIHKLD
     IPSFNWPVVE WPDVKYPFAQ NSRENAEAEK VALAAVEEAI VSSKKTGSSY GPVAALIVEP
     IQSEGGDNHA SPAFFQGLRD VTKKHGVFMI VDEVQTGVGA TGAFWAHSKW NLTSPPDFVT
     FSKKMQAAGF YHNIETRPSL PYRNYNTWMG DPARTLQARQ IIRTIQDHNL IQKTDKVGNY
     IYEKLFDLIE NGAGRGKIEK LRGENAGTFL AFDGRTAKVR DQLIMEMRKL GVHMGGCGDK
     ALRLRPMLVF EQKHADIFLD KLETALGQL