METXA_METZD
ID METXA_METZD Reviewed; 492 AA.
AC F7XKY8;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Mzhil_0824 {ECO:0000312|EMBL:AEH60686.1};
OS Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS (Methanohalophilus zhilinae).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX NCBI_TaxID=679901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002101; AEH60686.1; -; Genomic_DNA.
DR RefSeq; WP_013898125.1; NC_015676.1.
DR AlphaFoldDB; F7XKY8; -.
DR SMR; F7XKY8; -.
DR STRING; 679901.Mzhil_0824; -.
DR EnsemblBacteria; AEH60686; AEH60686; Mzhil_0824.
DR GeneID; 10822445; -.
DR KEGG; mzh:Mzhil_0824; -.
DR HOGENOM; CLU_028760_1_1_2; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 8770at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000006622; 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..492
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440295"
FT DOMAIN 47..354
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 375..432
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 436..492
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 315
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 348
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 221
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 492 AA; 54927 MW; EDA65B58A547D3E3 CRC64;
MKKGSLGIVE TKYYHLEEEL KLESGRKISD VTIAYEAYGT LNRDKNNVIL VCHALTGDAH
AAGWHKGDNK PGWWDILIGP GKCLDTDKYF IVCSNVIGGC RGSTGPSSID PETGKPYGLS
FPVITIKDMV NAQKKLLDHL GISSIYAVIG GSMGGLQVLQ WSVSYPDYIN KAIALAASAY
SSPQQIAFNE VARIAIISDP EWNKGNYYYS RQPSHGLALA RMIGHITYLS DESMREKFGR
ELQDRDRYNY DLSMDFQVES YLHYKGRSFT ERFDANSYLY ITKAVDYFDL TENGSLIDGL
KDIKAKCLII AVTSDWLYPP YQSKDIVMAL NANNVDVTYR EIESNYGHDA FLLEAGQLNY
VIGGFLNNIT VSDIMKLDVV TVQEDISIED AAQIMFDNGI THLPVVSDDE QIRGIITSWD
ISKAVALKFT TLDRILTKNV ITSRPDEGIE KCARKMQNNN ISALPVIDEN RKVIGIIGSD
EINKMIGNHR CT
