ID K2PLD9_9LACT Unreviewed; 396 AA.
AC K2PLD9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000313|EMBL:EKF52105.1};
DE EC=2.3.1.29 {ECO:0000313|EMBL:EKF52105.1};
GN ORFNames=C426_0578 {ECO:0000313|EMBL:EKF52105.1};
OS Lactococcus garvieae DCC43.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1231377 {ECO:0000313|EMBL:EKF52105.1, ECO:0000313|Proteomes:UP000006787};
RN [1] {ECO:0000313|EMBL:EKF52105.1, ECO:0000313|Proteomes:UP000006787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCC43 {ECO:0000313|EMBL:EKF52105.1,
RC ECO:0000313|Proteomes:UP000006787};
RX PubMed=23209230; DOI=10.1128/JB.01864-12;
RA Gabrielsen C., Brede D.A., Hernandez P.E., Nes I.F., Diep D.B.;
RT "Genome Sequence of the Bacteriocin-Producing Strain Lactococcus garvieae
RT DCC43.";
RL J. Bacteriol. 194:6976-6977(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:EKF52105.1}.
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; AMQS01000005; EKF52105.1; -; Genomic_DNA.
DR RefSeq; WP_003134862.1; NZ_AMQS01000005.1.
DR AlphaFoldDB; K2PLD9; -.
DR PATRIC; fig|1231377.3.peg.579; -.
DR eggNOG; COG0156; Bacteria.
DR Proteomes; UP000006787; Unassembled WGS sequence.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR010962; AONS_Archaea/Firmicutes.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01825; gly_Cac_T_rel; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EKF52105.1};
KW Ligase {ECO:0000313|EMBL:EKF52105.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:EKF52105.1}.
FT DOMAIN 42..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42323 MW; DFA3BF9D1CFB7F13 CRC64;
MTSKVLTQFL EKGLGDLKEK GLLNTIDVLD SANGPEITVA GKKMINLASN NYLGFATRPE
LIQATKDATD KYGAGAGAVR TINGTLDIHI ELEKTIAEFK GTEAAIAFQS GFNCNMGAIS
AVMKKGDAIL SDELNHASII DGCRLSGAKI IRLKHQDMAD LEAKAKEATE SGEYNKVMYI
TDGVFSMDGD VAKLPEIVKI AEKYDLITYV DDAHGSGVMG GGAGTVKHFG LQDKIDFQIG
TLSKAIGVVG GYVAGTQLLV DWLKSQGRPF LFSTSLTPGA AAAAKEAFVL MHDHPEYVET
LWDNAKYFKA ELQKAGFDTG VSETPITPVI LGDEAKTQEF SKKLIENGVY VKPIVFPTVP
LGTGRVRAMP TAAHTKEMLD EAVAVFAKVG KEIGLI
//