ID METAA_GEOKU Reviewed; 302 AA. AC A0A0D8BWP6; DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2015, sequence version 1. DT 25-MAY-2022, entry version 33. 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 Synonyms=metA {ECO:0000312|EMBL:KJE28404.1}; GN ORFNames=LG52_1351 {ECO:0000312|EMBL:KJE28404.1}; OS Geobacillus kaustophilus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=1462; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 8005 / DSM 7263 / JCM 20319 / NBRC 102445 / NCIMB 8547 / NRRL RC NRS-81 / IAM 11001 / BD53; 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Et7/4; RA Filippidou S., Jeanneret N., Russel-Delif L., Junier T., Wunderlin T., RA Molina V., Johnson S.L., Davenport K.W., Chain P.S., Dorador C., Junier P.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. 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}. 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; LN871223; CTQ31226.1; -; Genomic_DNA. DR EMBL; JYBP01000003; KJE28404.1; -; Genomic_DNA. DR RefSeq; WP_014195890.1; NZ_JYBP01000003.1. DR AlphaFoldDB; A0A0D8BWP6; -. DR SMR; A0A0D8BWP6; -. DR EnsemblBacteria; KJE28404; KJE28404; LG52_1351. DR PATRIC; fig|1462.6.peg.1545; -. DR UniPathway; UPA00051; UER00074. DR Proteomes; UP000032522; Unassembled WGS sequence. 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:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro. 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; IPR005697; HST_MetA. 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. DR TIGRFAMs; TIGR01001; metA; 1. PE 1: Evidence at protein level; KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm; KW Methionine biosynthesis; Transferase. FT CHAIN 1..302 FT /note="Homoserine O-acetyltransferase" FT /id="PRO_0000440340" FT ACT_SITE 142 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT ACT_SITE 235 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT ACT_SITE 237 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT BINDING 163 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT BINDING 192 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT BINDING 249 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT SITE 111 FT /note="Important for acyl-CoA specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" FT SITE 192 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295" SQ SEQUENCE 302 AA; 35281 MW; E67E673AC17F5968 CRC64; MPINIPKDLP AKEILEQENI FVMDEERAYS QDIRPLNIII LNLMPEKEKA ETQLLRLLGN SPLQVNVTFL RPATHEPKTT SKHHLEQFYT IFPHIRHRKF DGMIITGAPV EQLPFEEVTY WDELTDIMEW TKTNVTSTLH ICWGAQAGLY YHYGIPKYPL PEKCFGVFNH TVEAKNVKLL RGFDDVFRMP HSRHTDVKRE DIEKVPDLTI LSMSDKAGVC LVASNDGRRI FLTGHPEYDA TTLKEEYERD LAKGLPIHIP ESYFPNDDPS QPPLNTWRSH ANLLFVNWLN YYVYQETPYE WE //