METAA_CLOK5
ID METAA_CLOK5 Reviewed; 309 AA.
AC A5N8M0;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=metA1 {ECO:0000312|EMBL:EDK33651.1};
GN OrderedLocusNames=CKL_1609 {ECO:0000312|EMBL:EDK33651.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK33651.1; -; Genomic_DNA.
DR RefSeq; WP_012102004.1; NC_009706.1.
DR AlphaFoldDB; A5N8M0; -.
DR SMR; A5N8M0; -.
DR STRING; 431943.CKL_1609; -.
DR EnsemblBacteria; EDK33651; EDK33651; CKL_1609.
DR KEGG; ckl:CKL_1609; -.
DR eggNOG; COG1897; Bacteria.
DR HOGENOM; CLU_057851_0_1_9; -.
DR OMA; WLWFCYQ; -.
DR OrthoDB; 1601420at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000002411; 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: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; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440339"
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; 36482 MW; 1BEB7B4822FF6CF1 CRC64;
MPIKIKDDLP AAEILNSENI FIMPENVAFH QDIRPLKIAI LNLMPIKITT EVQLLRLIGN
TALQIEIELL HLKTHVCKNT SEEYLTNFYR TFDEIKNEKF DGLIITGAPI EQLEFSRVNY
WEELKDIMEW SKCHVYSTLH ICWGAQAGLY YHYGIPKYIL KEKLFGVFKH EVTEEKEKLV
RGFDDEFYVP HSRYTEVKRE DVEKVKELTI LAQSKKAGVY LILDNKGRRI FVTGHSEYDP
LTLKDEYMRD ISKGEDIKMP ENYFPDDNPD RKPVVKWRSH ADLLFSNWLN YYVYQETPYD
LSEMPPSFL
