ID   G0HL25_THES4            Unreviewed;       445 AA.
AC   G0HL25;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEK73378.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AEK73378.1};
GN   OrderedLocusNames=GQS_07400 {ECO:0000313|EMBL:AEK73378.1};
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73378.1, ECO:0000313|Proteomes:UP000000874};
RN   [1] {ECO:0000313|EMBL:AEK73378.1, ECO:0000313|Proteomes:UP000000874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX   PubMed=21914870; DOI=10.1128/JB.05851-11;
RA   Wang X., Gao Z., Xu X., Ruan L.;
RT   "Complete genome sequence of Thermococcus sp. strain 4557, a
RT   hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT   area.";
RL   J. Bacteriol. 193:5544-5545(2011).
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|RuleBase:RU003560}.
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DR   EMBL; CP002920; AEK73378.1; -; Genomic_DNA.
DR   RefSeq; WP_014013060.1; NC_015865.1.
DR   AlphaFoldDB; G0HL25; -.
DR   STRING; 1042877.GQS_07400; -.
DR   GeneID; 11016155; -.
DR   KEGG; the:GQS_07400; -.
DR   PATRIC; fig|1042877.9.peg.1440; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OrthoDB; 6534at2157; -.
DR   Proteomes; UP000000874; Chromosome.
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   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; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AEK73378.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AEK73378.1}.
SQ   SEQUENCE   445 AA;  49422 MW;  746A114ADDA22B06 CRC64;
     MVVRPNVKEL PGPKAKEVIE KNFEALAVTT QDPETLPIVI DHGDGILVYD VDGNTFYDFG
     SGVGVLNVGH AHPRVVEAVK RQAEKFTHFA LNDFFYENAV ILAQKLAELA PGDFPKKVVY
     QNSGAEANEA MMKLVKYGTG RKRFIAFYHA FHGRSQAVLS LTASKWVQQD RFFPTMPGVE
     HIPYPNPYRN PWHIDGYAEP DELVNRVIEF IEEYVFRHVP PHEVGAIVFE PIQGEGGYVV
     PPKNFFKELK KLADNYGILL ADDEVQMGVG RTGKFWAIEH FDVAPDTIQF GKAIGGGIPL
     AGVVHRADIA FDKPGRHAST FGGNPVAIAA GIEVVEIVKE LLPHVQEVGD YLHKRLEELL
     EKYEVIGDAR GLGLAQAVEI VKSKDTKEKN PELRDRIVKE AVKRGLILLG CGDNSIRFIP
     PLTISKEEID VAMEIFEEAL KAALQ
//