METAA_METAX
ID METAA_METAX Reviewed; 309 AA.
AC M9SGV8;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 41.
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 ORFNames=MMALV_06490 {ECO:0000312|EMBL:AGI85388.1};
OS Methanomethylophilus alvus (strain Mx1201).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Candidatus Methanomethylophilaceae;
OC Candidatus Methanomethylophilus.
OX NCBI_TaxID=1236689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mx1201;
RX PubMed=23209209; DOI=10.1128/jb.01867-12;
RA Borrel G., Harris H.M., Tottey W., Mihajlovski A., Parisot N.,
RA Peyretaillade E., Peyret P., Gribaldo S., O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomethylophilus alvus' Mx1201, a
RT methanogenic archaeon from the human gut belonging to a seventh order of
RT methanogens.";
RL J. Bacteriol. 194:6944-6945(2012).
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; CP004049; AGI85388.1; -; Genomic_DNA.
DR RefSeq; WP_015504536.1; NC_020913.1.
DR AlphaFoldDB; M9SGV8; -.
DR SMR; M9SGV8; -.
DR STRING; 1236689.MMALV_06490; -.
DR EnsemblBacteria; AGI85388; AGI85388; MMALV_06490.
DR GeneID; 41321438; -.
DR KEGG; max:MMALV_06490; -.
DR eggNOG; arCOG00090; Archaea.
DR HOGENOM; CLU_057851_0_1_2; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 37704at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000012672; 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:InterPro.
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; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440344"
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 /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT BINDING 249
FT /ligand="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 309 AA; 35899 MW; 96797D062060DE02 CRC64;
MPIKVPNDLP AATVLENENM FVMRENRAAS QDIRPLDLLI LNLMPTKVET EIQIMRLLSN
SPLQVNVRLL QMSSHVSKNT SQEYLDRFYD RFDDVKSRKW DGMIITGAPV ENIDFEEVDY
WDELCQIMEW SKKNVFSTLH ICWGAQAGLN YHYGIPKYPL ESKMSGVFAH KAIVRDDPLL
RGCDDIFWFP HSRHTEVRAE DIIRNPHLHI IAVSDEAGVG IVVSENSGQV FVTGHMEYDA
KTLSYEYYRD LGKGMNPHIP YHYFPDDDPS KDPVMNWRST ANLIFTNWLN YYVYQRVPYD
INEIGKDSE
