ID A0A0D2ENC0_9EURO Unreviewed; 521 AA.
AC A0A0D2ENC0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=Z517_10627 {ECO:0000313|EMBL:KIW75882.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW75882.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW75882.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75882.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846975; KIW75882.1; -; Genomic_DNA.
DR RefSeq; XP_013279690.1; XM_013424236.1.
DR AlphaFoldDB; A0A0D2ENC0; -.
DR STRING; 1442368.A0A0D2ENC0; -.
DR GeneID; 25310117; -.
DR VEuPathDB; FungiDB:Z517_10627; -.
DR HOGENOM; CLU_016922_12_0_1; -.
DR OrthoDB; 177625at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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:KIW75882.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Transferase {ECO:0000313|EMBL:KIW75882.1}.
SQ SEQUENCE 521 AA; 57613 MW; 03E29976ECD26CAD CRC64;
MASFLRASAG LRSVSRLATP ARSLLRPTPF RALATSPEKR TATAVAQAHV ESPSMETAFF
PDEPVGPTVV TPIPGPQSQK AIAELHKVFD TRSLNMLANY QQSYANYIAD PDGNVLLDVY
AQIASIPVGY NNPSLLLAAT SPEMASAIIN RPALGNFPSH DWASILQTGI LRVAPKGLDQ
VFTATAGSDA NETAFKAAFM WKRQQERGGR DVEFTAEEIE STMKNQKPGS PDMSIMSFKT
AFHGRLFGTL STTRSKPIHK IDIPAFDWPQ CSFPSLKYPL EQYAEENAVE EKRCLEEAEH
IIKTYHNPVA AVIVEPIQSE GGDNHASPAF FRGLREITRR NNVLLIVDEV QTGVGATGKF
WAHDHWNLED PPDMVTFSKK AQTAGYYFGN PDLRPNKPYR QFNTWMGDPA RAILFRAIIN
EIERLNLVEN TATVGDYLYA GIESLAQQYP QQFQNLRGKG QGTFIAFDNP KRDEFLAKAK
TFGINIGGSG ASAVRLRPML IFQKHHADIL LDAFEKLAKS L
//