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Database: UniProt
Entry: A0A2K0WHR3_GIBNY
LinkDB: A0A2K0WHR3_GIBNY
Original site: A0A2K0WHR3_GIBNY 
ID   A0A2K0WHR3_GIBNY        Unreviewed;       502 AA.
AC   A0A2K0WHR3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=FNYG_04848 {ECO:0000313|EMBL:PNP81822.1};
OS   Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP81822.1, ECO:0000313|Proteomes:UP000236664};
RN   [1] {ECO:0000313|EMBL:PNP81822.1, ECO:0000313|Proteomes:UP000236664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS10214 {ECO:0000313|EMBL:PNP81822.1,
RC   ECO:0000313|Proteomes:UP000236664};
RA   Gardiner D.M., Obanor F., Kazan K.;
RT   "Genome of Fusarium nygamai isolate CS10214.";
RL   Submitted (JUN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNP81822.1}.
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DR   EMBL; MTQA01000064; PNP81822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K0WHR3; -.
DR   STRING; 42673.A0A2K0WHR3; -.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000236664; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236664};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   502 AA;  55187 MW;  781685603678E648 CRC64;
     MSAFRAGMAA RPAVQAARAA VCRSFATSRS MRMAAVSEKT VFAGEPEAPT VKTTIPGPKT
     KSHMDELTKV FDTRSANMLV DYTKSKGNYI ADPDGNVLLD VFAQIASIAV GYNNPALLKA
     ASSPEMVNAI VNRPALGAFP SHDWADLLKS SLLTVAPKGL DNVFTAMAGS DANETAYKAA
     FMWRRQQERG GPEVDFSTKE LDSAMDNHAP GSPNLSILSF KTGFHGRLFG SLSTTRSKAI
     HKVDIPAFDW PQATFPKLKY PLEENVEENK KIEQASLDEV EHLIKNWHLP PCAVVVEPVQ
     SEGGDNHASP DFFRKLRALT KKHNILLIVD EVQTGIGATG KFWAHEHWNL ETPPDIVTFS
     KKAQAAGFYY GDPAIRPNKP YRQFNTWMGD PARAILFKAI VDEINKNDLV NHTARVGDRL
     FKDLESLSKK YPGQIENLRG KGQGTFIAFD SPKRDQFLGE AKKLGVNIGG SGASAVRLRP
     MLIFQQKHAD ILVDTIEKIV KQ
//
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