ID A0A0F2KL32_9PROT Unreviewed; 428 AA.
AC A0A0F2KL32;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KJR61428.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KJR61428.1};
GN ORFNames=VY88_32625 {ECO:0000313|EMBL:KJR61428.1};
OS Azospirillum thiophilum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=528244 {ECO:0000313|EMBL:KJR61428.1, ECO:0000313|Proteomes:UP000033623};
RN [1] {ECO:0000313|EMBL:KJR61428.1, ECO:0000313|Proteomes:UP000033623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21654 {ECO:0000313|EMBL:KJR61428.1,
RC ECO:0000313|Proteomes:UP000033623};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Azospirillum thiophilum strain DSM 21654T.";
RL Submitted (MAR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR61428.1}.
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DR EMBL; LAEL01000008; KJR61428.1; -; Genomic_DNA.
DR RefSeq; WP_045586206.1; NZ_LAEL01000008.1.
DR AlphaFoldDB; A0A0F2KL32; -.
DR STRING; 528244.AL072_15340; -.
DR KEGG; ati:AL072_15340; -.
DR PATRIC; fig|528244.3.peg.6518; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000033623; 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; 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 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:KJR61428.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KJR61428.1}.
SQ SEQUENCE 428 AA; 45262 MW; 4AF02715334E6569 CRC64;
MSNQSYVARR EAAVSRGVSA GLPIYVERAE NSELWDIEGK RFIDFAGGIA VLNTGHRHPK
VMAAVKAQLD RFTHTCAMVT PYESYVELAE KLNTLVPGPT PKKTAFFTSG AEAVENAVKI
ARAATGRPGV VAFSGGFHGR TLLTMGLTGK VVPYKVGFGP FPAEIFHVPF PNPYRGISEA
ESLKALDNLF KSDVDPARVA AIIIEPVQGE GGFNIASPAF LQSLRAVCDT HGIVMIVDEI
QTGFARTGKL FAVEHAGIEP DLVTMAKSLA GGFPLSAVTG KAHLMDAPVP GGLGGTYGGN
PLATSAALAV IEAIEEEKLC ERAQVIGERI ADRFRAMGQR NSLPVVGDVR NLGAMVAMEL
VTDRATKEPA ADLTKALVAK AAEKGLILLS CGTYANVIRV LVPLTASDAL IDEGLDIIER
SLEELVSA
//
