ID E6ZTC5_SPORE Unreviewed; 507 AA.
AC E6ZTC5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
GN Name=GatA {ECO:0000313|EMBL:CBQ70482.1};
GN ORFNames=sr12378 {ECO:0000313|EMBL:CBQ70482.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70482.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70482.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00000442};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FQ311441; CBQ70482.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZTC5; -.
DR EnsemblFungi; CBQ70482; CBQ70482; sr12378.
DR VEuPathDB; FungiDB:sr12378; -.
DR eggNOG; KOG1405; Eukaryota.
DR HOGENOM; CLU_016922_12_0_1; -.
DR OrthoDB; 177625at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006536; P:glutamate metabolic process; IEA:EnsemblFungi.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00699; GABAtrns_euk; 1.
DR PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:CBQ70482.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBQ70482.1}.
SQ SEQUENCE 507 AA; 55630 MW; 7A61CAA15A50CAF8 CRC64;
MIASRASTTA RACARISSVL RQHQRRSLAT VASSLFPGEP SAPHLVTPAI PGPKSKELSD
RIGIFQENRA HGFVVDYAKS QGNWIADADG NVLLDMFAQI ASIAIGYNNP DLIALAKTDE
FITATMNRAA LGSFPPTNWQ ELVETGLGTV KPKGLDNIFT AMCGSCANEN AFKASFMAYR
ARERGEQAQF TPEEMQSCMK NQSPGSPDLS ILSFTSAFHG RLFGSLSATR SKAIHKLDIP
SFNWPVVEWP DVKYPLSQNA RENAEAEKVA LAAVEEAIVN SRKAGSPNGP VAALIVEPIQ
SEGGDNHASP AFFQGLRDVT KKHGVFMIVD EVQTGVGATG AFWAHDKWNL TSPPDFVTFS
KKMQAAGFYH NIDTRPSMPY RNYNTWMGDP TRTLQARQII RTIQDHNLVE KTDKVGNYIY
EKLTDVIENG AGRGKVEKLR GENAGTFLAF DGKTPEVRDK LIMEMRKLGV HMGGCGDKAV
RLRPMLVFEQ KHADLFLEKL DKALGQL
//
