METXA_METPE
ID METXA_METPE Reviewed; 490 AA.
AC B8GHE0;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Mpal_1207 {ECO:0000312|EMBL:ACL16545.1};
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:0-0(2015).
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; CP001338; ACL16545.1; -; Genomic_DNA.
DR RefSeq; WP_012617864.1; NC_011832.1.
DR AlphaFoldDB; B8GHE0; -.
DR SMR; B8GHE0; -.
DR STRING; 521011.Mpal_1207; -.
DR EnsemblBacteria; ACL16545; ACL16545; Mpal_1207.
DR GeneID; 7271485; -.
DR KEGG; mpl:Mpal_1207; -.
DR eggNOG; arCOG00627; Archaea.
DR HOGENOM; CLU_028760_1_1_2; -.
DR OMA; NPQPGWW; -.
DR OrthoDB; 8770at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000002457; 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; -; 2.
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..490
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440291"
FT DOMAIN 47..353
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..490
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 490 AA; 52981 MW; 1E6BA1DC2FE86413 CRC64;
MQRGSVGIST TSTFTLATPL LLESGASLFS VQIAYETYGT LNHDKSNAIL VCHALTGDAH
AAGHHGDESR PGWWDGVIGP GKAFDTDKYF VICSNVLGGC KGTTGPASQN PDTGKPYGTS
FPVVTIRDMV NVQKALIDHL GISQLFAVAG GSMGGMQVLQ WMVSYPSMVR KAIAIAATGS
STPQQIAFNE VGRKAITADP AWCGGDYYGK EHPVKGLSLA RMVAHITYLS DASMHTKFGR
ALQDREFRGF DFDTEFQVES YLHHQGTSFT KRFDANSYLY LTKAVDYFDL SVDDSLISGF
APTKATVLII SVTSDWLYPP YQSQEIVSAL SANECDVHYC ELRSQFGHDA FLIETGQLNY
SISRFLDHTL VRDVMNTQVP VISEQSTIAV AARMMITQGV NHLPVLAPDQ SLVGIVTSWD
IANAVACGYT SLDQIMSSQV ITTTGDETIE VAASRMEQHR ISALPVIDQA QHVIGLISSD
GLSKLIGRGP
