ID   A0AAN0P3U1_LACLK        Unreviewed;       376 AA.
AC   A0AAN0P3U1;
DT   02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2024, sequence version 1.
DT   27-NOV-2024, entry version 2.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   Name=arcT {ECO:0000313|EMBL:ADA65790.1};
GN   OrderedLocusNames=LLKF_2218 {ECO:0000313|EMBL:ADA65790.1};
OS   Lactococcus lactis subsp. lactis (strain KF147).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA65790.1, ECO:0000313|Proteomes:UP000001886};
RN   [1] {ECO:0000313|EMBL:ADA65790.1, ECO:0000313|Proteomes:UP000001886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF147 {ECO:0000313|EMBL:ADA65790.1,
RC   ECO:0000313|Proteomes:UP000001886};
RX   PubMed=18039825; DOI=10.1128/aem.01850-07;
RA   Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA   van Hylckama Vlieg J.E.;
RT   "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT   isolates from plants identifies mechanisms of adaptation to the plant
RT   niche.";
RL   Appl. Environ. Microbiol. 74:424-436(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP001834; ADA65790.1; -; Genomic_DNA.
DR   RefSeq; WP_012898532.1; NC_013656.1.
DR   Proteomes; UP000001886; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR   PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ADA65790.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ADA65790.1}.
FT   DOMAIN          42..363
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   376 AA;  42696 MW;  152F880C9F04708B CRC64;
     MELVQFGCED WLNVWEKSAT IDIAQSTIDS LSLEEVLAFE EDNGEAFMLQ MMKEKFSYGW
     IEGSPAFKSE VAKLYKRVPE DNILSTNGAT GANFLTILGL IGQGDHVIAQ YPSYQQLYDW
     PKTLGAQVDY WHIKEENNWL PQIEELRRLV KSNTKLICLN NAAQPTGAIM SPKFLSEVVE
     IARSVDAYIL CDEVYLPLDE ETPYSPIADL YEKGISTNSI SKTYSVPGIR VGWVATQDRD
     LCNEFRKIRD YTLICTGVFD DAVAALVLKH KDKVLERARK IVKGNLSILK EWVENEPLVS
     MVYPNAVSVS FVKFEELDPT KTEDFAIQLL REKGVLIIPG NRFDLPGYAR IGYCTDETTL
     RQGLKLLSEF LREYQV
//