ID   R1GXL1_BOTPV            Unreviewed;       512 AA.
AC   R1GXL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=UCRNP2_88 {ECO:0000313|EMBL:EOD53111.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD53111.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB915654; EOD53111.1; -; Genomic_DNA.
DR   RefSeq; XP_007579416.1; XM_007579354.1.
DR   AlphaFoldDB; R1GXL1; -.
DR   STRING; 1287680.R1GXL1; -.
DR   KEGG; npa:UCRNP2_88; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   OMA; KTQVCGI; -.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000013521; 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; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
SQ   SEQUENCE   512 AA;  56115 MW;  885D7BE63E943226 CRC64;
     MSSFLRTASR LRPCASRAIA RPSAAIATPV SRQYASAAAA AASAPAGEQP FFPDEPAGPV
     VKGAIPGPQS AKAIEKLSKV FDTRSLNMMA DYRNSYGNYI ADLDGNVLLD VYAQIASIPV
     GYNNASLLLA SSSPEMASAI INRPALGNFP QHDWADILET GILKVAPKGL DQVFTAQSGS
     DANELAYKAA FMWKRRQQRG GPDVEFTPEE METAMNNTVP GAPKLSIMSF KAGFHGRLFG
     SLSTTRSKPI HKLDIPAFDW PQAPFPNLKY PLDQHAAENA AEEKRCLEET ERLIKEYHNP
     PAAIIIEPVQ SEGGDNHASP AFFNGLREIT KRNDVLMIVD EVQTGVGATG KFWAHEHWNM
     TTPPDMVTFS KKAQTAGYYF GNDDLRPNKP YRQFNTWMGD PARALLFRGI INEIERLGLV
     QNTAQTGDYL YAGLERLAQQ YPNEIQNLRG KGQGTFIAWD SPRRDEVLKN AKGAGINIGG
     SGAAAVRLRP MLIFQKHHAD IFLERLESVL KA
//