ID A0A0K1F8A0_9MICO Unreviewed; 418 AA.
AC A0A0K1F8A0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AKT50748.1};
GN ORFNames=ADJ73_04475 {ECO:0000313|EMBL:AKT50748.1};
OS Arsenicicoccus sp. oral taxon 190.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Arsenicicoccus.
OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT50748.1, ECO:0000313|Proteomes:UP000065578};
RN [1] {ECO:0000313|Proteomes:UP000065578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-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|RuleBase:RU003560}.
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DR EMBL; CP012070; AKT50748.1; -; Genomic_DNA.
DR RefSeq; WP_050347278.1; NZ_CP012070.1.
DR AlphaFoldDB; A0A0K1F8A0; -.
DR STRING; 1658671.ADJ73_04475; -.
DR KEGG; ars:ADJ73_04475; -.
DR PATRIC; fig|1658671.3.peg.904; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000065578; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; ORNITHINE AMINOTRANSFERASE; 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:AKT50748.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AKT50748.1}.
SQ SEQUENCE 418 AA; 43987 MW; C825C6B4BBB5D006 CRC64;
MTSLSPLLKQ ATPVVVDHAS GCWIHGQDGR DYLDFTTGIG VTSTGHCHPR VVEAAREQVG
KIIHAQYTTV MHQPLLDLTE RLGQVLPEGL DSVFYANSGS EAVESAVRLA RMATGRPNIV
VFQGGFHGRT VAAATLTTAG TRFAAGFSPL MGGVHMAPFP YAYRYGWDVD TAIDFALREL
DHLFATRTSP ADTAAFLIEP VLGDGGYLPT PPRFLQGLRE RADEHGILLV LDEVQAGCGR
TGRFWGHQHA DVAPDILLTA KGIASGFPIS AMAASEALMS RGWPGSQGGT YGGNAVAAAA
GCATLDVIRD EGLVDNARVR GDQLRAGLDA LAADVDAIGD VRGLGLMQGI EFTTADGRPD
AATALAVQQG TTAHGLLTLT CGPLGNVVRV MPALVVSEEE IELGLQRFRA TVEEVVPG
//