METAA_LEUMM
ID METAA_LEUMM Reviewed; 305 AA.
AC Q03V79;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295};
GN Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:28581482};
GN OrderedLocusNames=LEUM_1806 {ECO:0000312|EMBL:ABJ62893.1};
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000269|PubMed:28581482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC Rule:MF_00295}.
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DR EMBL; CP000414; ABJ62893.1; -; Genomic_DNA.
DR RefSeq; WP_010284094.1; NC_008531.1.
DR AlphaFoldDB; Q03V79; -.
DR SMR; Q03V79; -.
DR STRING; 203120.LEUM_1806; -.
DR EnsemblBacteria; ABJ62893; ABJ62893; LEUM_1806.
DR GeneID; 61177779; -.
DR KEGG; lme:LEUM_1806; -.
DR eggNOG; COG1897; Bacteria.
DR HOGENOM; CLU_057851_0_0_9; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000362; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03131; GATase1_HTS; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00295; MetA_acyltransf; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033752; MetA_family.
DR PANTHER; PTHR20919; PTHR20919; 1.
DR Pfam; PF04204; HTS; 1.
DR PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..305
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440343"
FT ACT_SITE 132
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 101
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 181
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ SEQUENCE 305 AA; 35543 MW; 7ED704DF248832B2 CRC64;
MSVILNNGLL KRESFVIGRF EVLEPTINIL LVNLMPNRLQ TEKQFTRLLS HLPINVRVTF
AVPSEHKIRH DTDAIMTNYV TLNDIWHKKF DGMIVTGAPV DRMKFEQIDY WDEFRHLLEW
RKTHVTESLF ACWAAYGAGY AERNFPVKAL SEKISGVFQA SQIFKRHSLL KDLENISMPQ
SRYFTVPNFG VARRLKVAGD DILGAFILRD EHVNSTYITG HFEYDTETLE NEYLRDIAID
PNTIKPKNYF YNNKPTNTWQ TYAEKFFVNW GELLMEKMTS SRSTIPTLNQ ERNKLGLGTS
QCKYL
