ID   G2SS12_LIGR2            Unreviewed;       425 AA.
AC   G2SS12;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AEN78960.1};
GN   OrderedLocusNames=LRC_17180 {ECO:0000313|EMBL:AEN78960.1};
OS   Ligilactobacillus ruminis (strain ATCC 27782 / RF3) (Lactobacillus
OS   ruminis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1069534 {ECO:0000313|EMBL:AEN78960.1, ECO:0000313|Proteomes:UP000001279};
RN   [1] {ECO:0000313|EMBL:AEN78960.1, ECO:0000313|Proteomes:UP000001279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27782 / RF3 {ECO:0000313|Proteomes:UP000001279};
RX   PubMed=21995554; DOI=10.1186/1475-2859-10-S1-S13;
RA   Forde B.M., Neville B.A., O'Donnell M.M., Riboulet-Bisson E.,
RA   Claesson M.J., Coghlan A., Ross R.P., O'Toole P.W.;
RT   "Genome sequences and comparative genomics of two Lactobacillus ruminis
RT   strains from the bovine and human intestinal tracts.";
RL   Microb. Cell Fact. 10:S13-S13(2011).
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; CP003032; AEN78960.1; -; Genomic_DNA.
DR   RefSeq; WP_014074101.1; NC_015975.1.
DR   AlphaFoldDB; G2SS12; -.
DR   STRING; 1069534.LRC_17180; -.
DR   GeneID; 29802983; -.
DR   KEGG; lrm:LRC_17180; -.
DR   PATRIC; fig|1069534.5.peg.1830; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   Proteomes; UP000001279; 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; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 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:0000313|EMBL:AEN78960.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001279};
KW   Transferase {ECO:0000313|EMBL:AEN78960.1}.
SQ   SEQUENCE   425 AA;  46524 MW;  A801693CFBC42698 CRC64;
     MESLYERSLK VFPPVAGRAT KIGAVSGQGS WLIDESGKKY LDFASGVAVV NCGHNHPKVV
     EAVEKQLHEL VHGGHNVVYY PKYVELAEKL VARVGKPGEY KVYFSNSGAE ANEGAVKLAL
     KATGRPGIIA FNGSFHGRTL LCASMTASSA LYRENYEPEL PQVYHADFPD VWNTDLTEQE
     EIERCLNSVH KIFTNLILPE RVACMVIEPV QGEGGYLPAP KRFIAELRKI CDEHGILLIF
     DEVQSGYGRT GYLFAKDYYG VQPDIFTSAK AIANGIPLSA VIGKTEYMDK WLAGSHGGTF
     GGNPLACAAG CAVLDVIDED FLEDVRKKGA FIRERLEDLK VTHSNVISSI RGIGMMNGVE
     FRKDGKPLPK IVSKVQEIAL SKGLILLNCG TFHNVIRLIP PLTATKEEIE QAIGIIDECL
     KEIEG
//