ID S4XAT8_9CORY Unreviewed; 447 AA.
AC S4XAT8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AGP29741.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:AGP29741.1};
GN ORFNames=A606_00430 {ECO:0000313|EMBL:AGP29741.1};
OS Corynebacterium terpenotabidum Y-11.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1200352 {ECO:0000313|EMBL:AGP29741.1, ECO:0000313|Proteomes:UP000014809};
RN [1] {ECO:0000313|EMBL:AGP29741.1, ECO:0000313|Proteomes:UP000014809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y-11 {ECO:0000313|EMBL:AGP29741.1,
RC ECO:0000313|Proteomes:UP000014809};
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Szczepanowski R., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium terpenotabidum Y-11 (=DSM
RT 44721).";
RL Submitted (JUN-2012) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003696; AGP29741.1; -; Genomic_DNA.
DR RefSeq; WP_020440106.1; NC_021663.1.
DR AlphaFoldDB; S4XAT8; -.
DR STRING; 1200352.A606_00430; -.
DR KEGG; cter:A606_00430; -.
DR PATRIC; fig|1200352.3.peg.81; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000014809; 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 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; 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; 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:AGP29741.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AGP29741.1}.
SQ SEQUENCE 447 AA; 46243 MW; EAC37BD37693A66A CRC64;
MQDLPSRLPQ QRSIVTDQLP GPVSAALAAR TAASVPRGIA PSLAAYVVDA DGGVLVDADG
NSFIDFASGI AVTSVGASNA KVVDAVAAAA AHFTHTNFTT SPYQSYVDVA EKLNEITPGD
HDKRTVLLNS GAEAVENAVK IARAFTGKPA VAVMDRAYHG RTNLTMAMTA KNVPYKSGFG
PFASDVYRVP MSYPLRDQLT GPEAAERTIW TMEKEIGSEN LSCVVIEPIQ GEGGFIAPAE
GFLPAIAEWC RANGVVFIAD EIQAGMCRTG DWFAVNHENV VPDILTIAKG VAGGMPLSAV
TGRAEIMDAS GPGSLGGTYA GNPVACAAAL AAIDEMETHD LAGRAREIEG IVREVLEPLV
DETAGRVAEV RGRGAMLAVE ITGADGRPDA AAVKKVAAAC QAAGVLILTC GLDGNVIRLL
PALVISESLL RDGLTVLAAA LRSEVGV
//