ID   G2RAD7_THETT            Unreviewed;       467 AA.
AC   G2RAD7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=THITE_2118631 {ECO:0000313|EMBL:AEO68869.1};
OS   Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS   terrestris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC   Thermothielavioides terrestris.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO68869.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO68869.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
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; CP003012; AEO68869.1; -; Genomic_DNA.
DR   RefSeq; XP_003655205.1; XM_003655157.1.
DR   AlphaFoldDB; G2RAD7; -.
DR   STRING; 578455.G2RAD7; -.
DR   GeneID; 11524047; -.
DR   KEGG; ttt:THITE_2118631; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000008181; Chromosome 4.
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:UP000008181};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  52088 MW;  9506DB072648BA5D CRC64;
     MSSFYSGWEP EGPSVKTEIP GPKAKAATTV LNEVFDTRSL NMLTDYSRSA GNYIVDADGN
     VLLDVYAQIA SIPLGYNNPA LRKAAQSDEM INGLINRPAL GNFPPLDWAE ILKTGILKVA
     PKGLNQVFTA MAGSDANETA YKAAFMWRRQ RDRGGPQVEF TEEEMQSAME NKSPGASQLS
     ILSFKSAFHG RLFGSLSTTR SKPIHKLDIP AFDWPQATFP KLKYPLDEHA AENAAIEQAA
     LDEVEHLIKN YHVPPCAVIV EPIQSEGGDN HASPAFFRGL REITRRHGVL LIVDEVQTGV
     GATGRFWAHE HWDLPHPPDM VTFSKKAQTA GYYFGNPELR PNKPYRQFNT WMGDPARALV
     FRAIIDEIER LDLVRHTARV GDYLYGKLER LAEKYPDEFQ NLRGKGMGTF IAFDNPRRDA
     FLARAKKFGI NIGGSGQSAV RLRPMLIFEE KHADILVDAL EKIVTSW
//