METXA_METST
ID METXA_METST Reviewed; 490 AA.
AC Q2NGH9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Synonyms=metX {ECO:0000312|EMBL:ABC57074.1};
GN OrderedLocusNames=Msp_0676 {ECO:0000312|EMBL:ABC57074.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57074.1; -; Genomic_DNA.
DR RefSeq; WP_011406274.1; NC_007681.1.
DR AlphaFoldDB; Q2NGH9; -.
DR SMR; Q2NGH9; -.
DR STRING; 339860.Msp_0676; -.
DR ESTHER; metst-q2ngh9; Homoserine_transacetylase.
DR EnsemblBacteria; ABC57074; ABC57074; Msp_0676.
DR GeneID; 41325251; -.
DR KEGG; mst:Msp_0676; -.
DR eggNOG; arCOG00627; Archaea.
DR HOGENOM; CLU_028760_1_1_2; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 8770at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000001931; 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..490
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440293"
FT DOMAIN 48..354
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 377..434
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT DOMAIN 438..490
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 317
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 350
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 490 AA; 55389 MW; BA580CB17C6854D7 CRC64;
MTYKKSLGNV STKYYKMKED LQLDTGNILE TPTIAYETYG KLNNEKSNVI LVCHALTGDA
HAAGWHDGDK KPGWWNIIIG PGKPLDTNRY FIICSNVLGS CKGTTGPCDI NPKTNKPYGL
DFPIITINDM VKAQKKLLDY LDINHLYAVV GGSMGGMQVL QWTITYPDMV RNAIMIASGA
YSTPQQIAFN AVQRRSIIED PNWKGGKYYE EGVSPEQGLS VARMIAHITY LSNESMYEKF
GRKLQDKNKF SYDFSTEFQV ESYLEHQGST FTKKFDANSY LYLTKALDYF EVRKNTSLEE
ALKPVKSRIL IMSITSDWLY THEHMEEIVM ALRANNVEVS YSRLNSEYGH DAFLIENGQM
NYIISNFLSK ARVKDVMSHT TLTLDYTADI KEAAELMMNC NKTHIPIVDD GKEIVGIITA
WDLSKAIATD ANSIDDIMTK NVLTCTEYDS LHKVIRKMKE HNISGLPVID KNHKVIGSIT
TAHISNLYEK
