METXA_METLZ
ID METXA_METLZ Reviewed; 487 AA.
AC A2SQW3;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Mlab_0545 {ECO:0000312|EMBL:ABN06719.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06719.1; -; Genomic_DNA.
DR RefSeq; WP_011832920.1; NC_008942.1.
DR AlphaFoldDB; A2SQW3; -.
DR SMR; A2SQW3; -.
DR STRING; 410358.Mlab_0545; -.
DR ESTHER; metlz-a2sqw3; Homoserine_transacetylase.
DR EnsemblBacteria; ABN06719; ABN06719; Mlab_0545.
DR GeneID; 4795912; -.
DR KEGG; mla:Mlab_0545; -.
DR eggNOG; arCOG00627; Archaea.
DR HOGENOM; CLU_028760_1_1_2; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 8770at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000365; 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; 3.10.580.10; -; 1.
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; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; CBS domain; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..487
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440289"
FT DOMAIN 45..352
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 373..430
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 434..487
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 313
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 487 AA; 53097 MW; D9881AEA8117FAE3 CRC64;
MLQDSVGEVT TKYHALSVPL SLECGVSLSG VRIAYERYGR ADGKNVILVC HPLTGDAHAA
GFHKGDTKPG WWDGIIGPGK ALDTNRYCVI AANVLGGCKG STGPSSEDPA TGKPYGTTFP
VITIRDMVHA EHQLLEDLGI SELYAVIGGS MGGMQAMQWS VEFPSFVRRI ICIASAGYTT
PMHIAFGAVG RAAIMSDPEW NGGNYPAEKK PNHGLSLARM MAHITYLSDE SMRTKFGRRL
QKQDAFGYGF DTEFSVESYL QHQGETFVER FDPNSYLYIT RAVDYYDLTK NGSLTEGLAA
TQAKFLIISV SSDWLYPPYL SQEIMLALTT NNREARYAEI VSPHGHDGFL LENAQLNYIV
GQFLTPMTVE DLMTNNPPSI QETSSIREAA ELMIGHEINH LPVVSGNGTL SGIVTSWDIA
KSVAGDFQDL AEIMTKDVIT IQRSDSLRLA ASLMEKHAIS ALPVVDDSNH VLGMLTSETL
SLSEVLQ
