ID   A0A1H4L1C7_9RHOB        Unreviewed;       425 AA.
AC   A0A1H4L1C7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:SEB64570.1};
GN   ORFNames=SAMN05519105_0994 {ECO:0000313|EMBL:SEB64570.1};
OS   Rhodobacter sp. 24-YEA-8.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1884310 {ECO:0000313|EMBL:SEB64570.1, ECO:0000313|Proteomes:UP000199640};
RN   [1] {ECO:0000313|EMBL:SEB64570.1, ECO:0000313|Proteomes:UP000199640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24-YEA-8 {ECO:0000313|EMBL:SEB64570.1,
RC   ECO:0000313|Proteomes:UP000199640};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNSK01000001; SEB64570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4L1C7; -.
DR   STRING; 1884310.SAMN05519105_0994; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000199640; Unassembled WGS sequence.
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:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:SEB64570.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199640};
KW   Transferase {ECO:0000313|EMBL:SEB64570.1}.
SQ   SEQUENCE   425 AA;  45325 MW;  A0DC4BFFFC89922D CRC64;
     MKNAEVAKRR EDAISRGVGM STQIYADRAE NAEVWDIEGN RYIDFAAGIA VVNTGHRHPK
     VIAAVKDQLD RFTHTCHQVL PYENYIRLAE RLNEAVPGDF KKKTIFVTTG AEAVENAIKI
     ARRATGRNAV IALGGAFHGR TFMGMTLTGK VEPYKKGFGA MMPDVFHVPC PQEIHGITTK
     DTLDGITKLF KNDVDPERVA AIIFEPVQGE GGFYPLPTDL IKALRALCDQ HGIVLIADEV
     QTGIGRTGAL FAMEAHGVAA DLTTMAKGLG GGFPISAVTG RADLMDASQP GGLGGTYAGN
     PLSVAAANAV LDVVEEEGLN ARATELGSRL KQKLEEIRAT TPEIIDIRGP GFMIAAEFGK
     PGTTEPDGDI VKRIIAEALK RGLILLSCGV YGNVVRFLAP LTIAEAHFTE ALGILEASVA
     AARQG
//