ID A0A0R1M5P0_9LACO Unreviewed; 445 AA.
AC A0A0R1M5P0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KRL03153.1};
GN ORFNames=FC81_GL000154 {ECO:0000313|EMBL:KRL03153.1};
OS Liquorilactobacillus capillatus DSM 19910.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL03153.1, ECO:0000313|Proteomes:UP000051621};
RN [1] {ECO:0000313|EMBL:KRL03153.1, ECO:0000313|Proteomes:UP000051621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL03153.1,
RC ECO:0000313|Proteomes:UP000051621};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRL03153.1}.
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DR EMBL; AZEF01000006; KRL03153.1; -; Genomic_DNA.
DR RefSeq; WP_057742010.1; NZ_AZEF01000006.1.
DR AlphaFoldDB; A0A0R1M5P0; -.
DR STRING; 1423731.FC81_GL000154; -.
DR PATRIC; fig|1423731.3.peg.160; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000051621; Unassembled WGS sequence.
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; 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:KRL03153.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000051621};
KW Transferase {ECO:0000313|EMBL:KRL03153.1}.
SQ SEQUENCE 445 AA; 48498 MW; 9E3775B0883FD480 CRC64;
MINNKSLLDD ESNVLAETAR IKYFNIVIDS GKGAIIKDIE GNEYIDLLAS ASAVNTGHAH
PHVVAAIQKQ AAKLIQYTPA YFANTPAAKL AQRLCKLAPI SGPKKMFWGN SGSDANDGII
KLARAYTKRP YLVSFMGAYH GATYGSLSLS AVSLNMTRKI GPLLPDVVKV PYPDPWQRTK
NESEEDFVAR MFAEFKRPFE TFLPAEETAL IIIEPIQGDG GIVKAPVEFI RKVADFAHKN
GILFAVDEVN QGLGRTGKWW SIQHFGVEPD LMSVGKSLAS GLPLSAVIGR TEIMDSLDAP
AHLFTTSGNP VTTAAAMATL DVIENEKLVQ RSALLGTEVE AFFKAEQAKH SFIGQCRIYG
LNGGIDIIDP VTHKPDGLAA TKLIYRIFKL GAIIISLKTN ILRFQPPLVI TEEQLHQAFK
IIAQAFSELE EGRLALPANA DDIGW
//
