MTXAW_RHOBA
ID MTXAW_RHOBA Reviewed; 623 AA.
AC Q7UG04;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Bifunctional methionine biosynthesis protein MetXA/MetW {ECO:0000305};
DE Includes:
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000305};
DE Short=HAT {ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transacetylase {ECO:0000305};
DE Short=HTA {ECO:0000305};
DE Includes:
DE RecName: Full=Protein MetW {ECO:0000305};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN Synonyms=metX {ECO:0000312|EMBL:CAD78525.1};
GN OrderedLocusNames=RB8222 {ECO:0000312|EMBL:CAD78525.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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: In the N-terminal section; belongs to the AB hydrolase
CC superfamily. MetX family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MetW family.
CC {ECO:0000305}.
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DR EMBL; BX294147; CAD78525.1; -; Genomic_DNA.
DR RefSeq; NP_868247.1; NC_005027.1.
DR AlphaFoldDB; Q7UG04; -.
DR SMR; Q7UG04; -.
DR STRING; 243090.RB8222; -.
DR ESTHER; rhoba-q7ug04; Homoserine_transacetylase.
DR EnsemblBacteria; CAD78525; CAD78525; RB8222.
DR KEGG; rba:RB8222; -.
DR PATRIC; fig|243090.15.peg.3962; -.
DR eggNOG; COG2021; Bacteria.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_028760_6_0_0; -.
DR InParanoid; Q7UG04; -.
DR OMA; HQGQKFT; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 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; IPR008220; HAT_MetX-like.
DR InterPro; IPR010743; Methionine_synth_MetW.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF07021; MetW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
DR TIGRFAMs; TIGR02081; metW; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..623
FT /note="Bifunctional methionine biosynthesis protein
FT MetXA/MetW"
FT /id="PRO_0000440306"
FT DOMAIN 77..385
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..619
FT /note="MetW"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 348
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 381
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 623 AA; 68950 MW; 445E62055967CCF5 CRC64;
MTSGRSTRVT MFESQASMGE PSNEDLSSTD DVRTDAPLAY AKYVTFDQSL PLERGGELPE
IRCCYETWGT LNDDGSNAVL VCHAVSGDSH AARHDEDDQP GWWDGLIGPG LPIDTDRLFV
VCPNVLGGCR GSTGPGDADP TSPDGKPYGA NFPRITIGDI VEAQKLLADH LGIRQWRAVV
GGSLGGHQVL QWINRYPDAA KTCVAIATSP RLNSQALGFD VIARNAIQTD PHYAGGQYYD
KDQRPDTGLA IARMLGHITY LSVEAMEAKF DPDRHDPRQI ASQFEQRFSI GSYLAHQGQK
FTTRFDANSY VTLSMAMDLF DLGGTRLKLM ETFDEATCDF LLISFSSDWL FPPAQSREIV
NALTALDKRV TYAEITTNAG HDAFLIAKDI ATYGPLIRER LRDTETHPAV PSDITLNVDE
ESILEIIPAG SSVLDLGCGN GQLLAAIRDR HRTPGPPTTE HRLMGVEVAQ ENLLATAMRG
IDVIDYDLNH GLPAFIDDQF DYVILNATLQ AVENVVELLN EMLRVGRHAI ISFPNFAYRQ
LRDHYVTHGR SPKAPGEFDF DWHNTPNRRF PTIADVRDLL GQLNVVIDEE VFWDVDQGQR
IEPDNDPNLN ADTAVIAFHR ENR
