METXA_METFP
ID METXA_METFP Reviewed; 493 AA.
AC K2QXP6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
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 ORFNames=A994_10634 {ECO:0000312|EMBL:EKF85068.1};
OS Methanobacterium formicicum (strain DSM 3637 / PP1).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1204725;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3637 / PP1;
RX PubMed=23209223; DOI=10.1128/jb.01829-12;
RA Gutierrez G.;
RT "Draft genome sequence of Methanobacterium formicicum DSM 3637, an
RT archaebacterium isolated from the methane producer amoeba Pelomyxa
RT palustris.";
RL J. Bacteriol. 194:6967-6968(2012).
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; AMPO01000010; EKF85068.1; -; Genomic_DNA.
DR RefSeq; WP_004031585.1; NZ_AMPO01000010.1.
DR AlphaFoldDB; K2QXP6; -.
DR SMR; K2QXP6; -.
DR EnsemblBacteria; EKF85068; EKF85068; A994_10634.
DR PATRIC; fig|1204725.3.peg.2139; -.
DR OrthoDB; 8770at2157; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000007360; Unassembled WGS sequence.
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; Repeat; Transferase.
FT CHAIN 1..493
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440288"
FT DOMAIN 47..356
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..493
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 317
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 350
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 221
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 493 AA; 54933 MW; 508BAECF86D44DB3 CRC64;
MKKESVGVVE TKHYNLSEEL ILDGGDSLKD VTIAYETYGT LNKQKSNAIL VCHALSGNAH
VAGWHEGDRK PGWWDNIIGP GKCLDTDRYF IICSNVLGGC QGSTGPSSLN PETGKQYALE
FPIITIKDMV KAQKKLIDHL QIKQLFSVVG GSMGGMQVLQ WCVSYPDMVR SAIPIATTSY
SSPQQIAFNE VGRRAIISDP HWNEGNYYEG EFPDSGLALA RMIGHITYLS NESMYEKFGR
RLQDKEEYSF DFSTDFEVES YLHYQGDTFT KRFDANSYLY ISKAIDYFDL TENGTVSLSE
ALKNVKARVL VISVDSDWLY TPAESKEIVM AMTANEVDVS YCQIKSSYGH DAFLLEAGQL
SYIINGFFSE TLVVDVMTIH AATITEDSSI EEAAELMLDE KVTHLPVVSE DYRMLGIVTA
WDISKAVALK YDKLDQIMTR DVVTALPQDP IELAARKMRK HNISSLPVVN DQGNVLGLIT
TDHISTLIAG DKY
