ID   Q67RU2_SYMTH            Unreviewed;       457 AA.
AC   Q67RU2;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAD39601.1};
GN   OrderedLocusNames=STH616 {ECO:0000313|EMBL:BAD39601.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD39601.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD39601.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39601.1; -; Genomic_DNA.
DR   RefSeq; WP_011194749.1; NC_006177.1.
DR   AlphaFoldDB; Q67RU2; -.
DR   STRING; 292459.STH616; -.
DR   KEGG; sth:STH616; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000000417; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; IPR004632; 4NH2But_aminotransferase_bac.
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; TIGR00700; GABAtrnsam; 1.
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.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:BAD39601.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW   Transferase {ECO:0000313|EMBL:BAD39601.1}.
SQ   SEQUENCE   457 AA;  49441 MW;  BB5EE75AD7914CE5 CRC64;
     MTQTTRYVRL VTEVPGPRSR ELMARKERVV ANALSIHVPV AIQEARGALV TDVDGNVFID
     LAGGMGCMNV GHSHPRVVEA IQRSAAQFTH TDFSVIMYES YIRLAERLAA LAPGDFPKKA
     CFFNSGAEAV ENAIKIARKY TGRRAIIALE GAFHGRTNLA MALTSKVKPY KEGFGPFAPE
     IYRVPTPYTY RRPAGMSEAE YVRFCADALE RALITHVSPD EVAAIILEPV QGEGGFIPLH
     PDYLARVSQL ARKHGFLIIA DEIQSGFGRT GTFFASEQLG LVPDLICVGK SLAAGMPLSG
     VIGRAEVMDA PEDSTIGGTY VGNPVACDAA HAVLDIMEEE GLVSRARAIG DLMRRRFQEL
     AVQLESIPGS RLQIGEIRGL GAMLGVELVT DRATRAPATA EAAEVVKRAW QRGVVVVKCG
     IYGNTLRMLL PLVITDDQLN EALDIIGQIC TEIARGE
//