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}. 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; 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 //