METXA_SULAO
ID METXA_SULAO Reviewed; 368 AA.
AC E0UR96;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN OrderedLocusNames=Saut_0857 {ECO:0000312|EMBL:ADN08906.1};
OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS OK10).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=563040;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10;
RX DOI=10.4056/sigs.1173118;
RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10T).";
RL Stand. Genomic Sci. 3:194-202(2010).
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_00296,
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_00296,
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_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; CP002205; ADN08906.1; -; Genomic_DNA.
DR RefSeq; WP_013326662.1; NC_014506.1.
DR AlphaFoldDB; E0UR96; -.
DR SMR; E0UR96; -.
DR STRING; 563040.Saut_0857; -.
DR EnsemblBacteria; ADN08906; ADN08906; Saut_0857.
DR KEGG; sua:Saut_0857; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_7; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000007803; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..368
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440299"
FT DOMAIN 43..354
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 348
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 368 AA; 41872 MW; 2F59A9D144E2BA4D CRC64;
MSLNLQTYTE HFTNPLYLES GRILEPYDIT YETYGTMNED KSNVVVVCHA LTGSHHAAGL
YEDETKPGWW DGFIGSGKAI DTDKYFVICS NVIGSCFGST GPMSLQHPYQ EPYRYKFPVV
SIKDMVKAQR ILFDRLDIHR VHAIVGGSMG GMQALQFAIH YPNFANKIIA LATTHATQPW
AIAFNKVAQE SILNDPDFKQ GYYDPDLLKE QGLSGMAVGR MAGHISFLSH ESMREKFGRD
YKLTDGLYEL FGKFQVESYL EYNGYNFTKW FDPLAYLYIT KAINIYDLSR GFDSLAEALK
RVTSALYLVS FKNDLLFKNF EMKEIADELD KIGNKNHSYI DVKSDYGHDA FLVELNKFEN
HVKDALNG
