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 07-JUN-2017, entry version 21. DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295}; DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|Ref.1}; DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|Ref.1}; 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|Ref.1}; 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 / NCIMB 8547 / NRRL NRS-81 / RC IAM 11001; RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A., RA Petit J.-L., Darii E., Bazire P., Vergne C., Brewee C., Debard A., RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., RA Vallenet D., Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., RA de Berardinis V.; RT "Parallel evolution of two non-homologous isofunctional enzyme RT families in the methionine biosynthesis pathway."; RL Nat. Chem. Biol. 0:0-0(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., RA Junier P.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L- CC homoserine, forming acetyl-L-homoserine. {ECO:0000255|HAMAP- CC Rule:MF_00295, ECO:0000269|Ref.1}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-homoserine = CoA + O-acetyl-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|Ref.1}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo 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 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:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:UniProtKB-HAMAP. 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; Homserine_suc_trans. DR InterPro; IPR033752; HTS_family. DR PANTHER; PTHR20919; PTHR20919; 1. DR PANTHER; PTHR20919:SF1; PTHR20919:SF1; 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; Complete proteome; KW Cytoplasm; Methionine biosynthesis; Transferase. FT CHAIN 1 302 Homoserine O-acetyltransferase. FT /FTId=PRO_0000440340. FT ACT_SITE 142 142 Acyl-thioester intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00295}. FT ACT_SITE 235 235 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00295}. FT ACT_SITE 237 237 {ECO:0000255|HAMAP-Rule:MF_00295}. FT BINDING 163 163 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00295}. FT BINDING 192 192 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00295}. FT BINDING 249 249 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00295}. FT SITE 111 111 Important for acyl-CoA specificity. FT {ECO:0000255|HAMAP-Rule:MF_00295}. FT SITE 192 192 Important for substrate specificity. FT {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 //