METAA_METII
ID METAA_METII Reviewed; 305 AA.
AC R9T6W8;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=MMINT_11300 {ECO:0000312|EMBL:AGN26470.1};
OS Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX NCBI_TaxID=1295009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Issoire-Mx1;
RX PubMed=23846268; DOI=10.1128/genomea.00453-13;
RA Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT human feces.";
RL Genome Announc. 1:142-142(2013).
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; CP005934; AGN26470.1; -; Genomic_DNA.
DR RefSeq; WP_020448995.1; NC_021353.1.
DR AlphaFoldDB; R9T6W8; -.
DR SMR; R9T6W8; -.
DR STRING; 1295009.MMINT_11300; -.
DR EnsemblBacteria; AGN26470; AGN26470; MMINT_11300.
DR GeneID; 41323527; -.
DR KEGG; mer:MMINT_11300; -.
DR HOGENOM; CLU_057851_0_1_2; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 37704at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000014070; 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..305
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440345"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT ACT_SITE 235
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 247
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 305 AA; 35694 MW; 7D6E546067129C3F CRC64;
MPINIPDDLP AASILESEKI FVMNENRARH QDIRPLEILI FNLMPSKVET ETQILRLLSN
SPIQIDIDLL RTETYISKHT SQDYLQHFYK TFNEIKNKKY DGMIITGAPV ENMPYESVKY
WKEFCEILDW SLTNSFSTMH ICWGALAALY YHYGIPKHPL DEKISGIYAH VPLEYYHPLL
RGFDDVFYMP HSRYMTVKES DLKGDLKVLA RSEETGPAII MSDKLRQVFV TGHLEYDTMT
LANEYKRDLE KGLHPVIPEN YFPDNDPNAA PKKLWRSHAS LLFSNWLNYY VYQQTPYDLL
KIGRS
