ID A0A0H4QKL5_9LACO Unreviewed; 456 AA.
AC A0A0H4QKL5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AKP67263.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:AKP67263.1};
GN ORFNames=ABM34_06730 {ECO:0000313|EMBL:AKP67263.1};
OS Companilactobacillus ginsenosidimutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1007676 {ECO:0000313|EMBL:AKP67263.1, ECO:0000313|Proteomes:UP000036106};
RN [1] {ECO:0000313|Proteomes:UP000036106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EMML 3041 {ECO:0000313|Proteomes:UP000036106};
RA Kim M.K., Im W.-T., Srinivasan S., Lee J.-J.;
RT "Lactobacillus ginsenosidimutans/EMML 3141/ whole genome sequencing.";
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; CP012034; AKP67263.1; -; Genomic_DNA.
DR RefSeq; WP_048704456.1; NZ_CP012034.1.
DR AlphaFoldDB; A0A0H4QKL5; -.
DR STRING; 1007676.ABM34_06730; -.
DR KEGG; lgn:ABM34_06730; -.
DR PATRIC; fig|1007676.4.peg.1342; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000036106; 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 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; 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 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:AKP67263.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AKP67263.1}.
SQ SEQUENCE 456 AA; 50313 MW; 1A815CAE1E8B9C17 CRC64;
MEAKKVDHNH EKDKRLIERE NQYLASAERI NYYDLVIDSA HGAVLKDVDG NEYIDLLASA
SAINVGHTND LVVKAIQDQA EKLIHYTPSY FHHEPEQQLA EKLAKLAPGP TPKKVIFGNS
GSDANDAIIK FARAYTGRQY MVSYMNSYHG STYGSMALSG VSLNMTRKMG PLMPGVVHVP
YPDLYRTEPG ETEHDVAVRF FEAFKQPFES FLPADEVAAV LIEPIQGDGG LVKAPEEYMQ
MVYKFCHDNG ILFAVDEVNQ GMGRTGHMWG IENYHDIEPD LISVGKSIAS GMPLSAVVGK
ADVMNSLGSP AHTFTTAGNP VCCAAALATL EVLEKDSLIE KSKRDGEYAK ERFTEMQSRH
PNIGDVRMFG LNGGIELVED QETKVPDADF ATKVITYAFE HGVVIITLRG NILRFQPPLV
ITREELDQAL DVLDDAFTAV ENGEVSLPDT DSKIGW
//
