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METXS_PSEU2
ID   METXS_PSEU2             Reviewed;         379 AA.
AC   Q4ZZ78;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=HST {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE            EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE   AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=HTS {ECO:0000255|HAMAP-Rule:MF_00296};
GN   Name=metXS {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN   OrderedLocusNames=Psyr_0474;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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 a succinyl group from succinyl-CoA to L-homoserine,
CC       forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296,
CC       ECO:0000269|PubMed:28581482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine;
CC         Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00296,
CC         ECO:0000269|PubMed:28581482};
CC   -!- ACTIVITY REGULATION: Requires MetW for activity.
CC       {ECO:0000269|PubMed:28581482}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; O-succinyl-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; CP000075; AAY35544.1; -; Genomic_DNA.
DR   RefSeq; WP_011266425.1; NC_007005.1.
DR   RefSeq; YP_233582.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZZ78; -.
DR   SMR; Q4ZZ78; -.
DR   STRING; 205918.Psyr_0474; -.
DR   ESTHER; psesm-METX; Homoserine_transacetylase.
DR   EnsemblBacteria; AAY35544; AAY35544; Psyr_0474.
DR   KEGG; psb:Psyr_0474; -.
DR   PATRIC; fig|205918.7.peg.493; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_6; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR32268; PTHR32268; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Transferase.
FT   CHAIN           1..379
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_0000231883"
FT   DOMAIN          51..360
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        323
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            325
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT                   ECO:0000305|PubMed:28581482"
SQ   SEQUENCE   379 AA;  41691 MW;  20504B84362B061B CRC64;
     MPTVFPHDSV GLVTPQTAHF SEPLALACGR SLPAYDLIYE TYGQLNAARS NAVLICHALS
     GHHHAAGFHS ADDRKPGWWD SCIGPGKPID TTKFFVVSLN NLGGCNGSTG PSSIDPDTGK
     PFGANFPVVT VEDWVNSQAR LADLLGIDTW AAVIGGSLGG MQALQWTISY PNRVRHCLAI
     ASAPKLSAQN IAFNEVARQA ILTDPEFHGG SFQERGVIPK RGLMLARMVG HITYLSDDSM
     GEKFGRGLKS EKLNYDFHSV EFQVESYLRY QGEEFSGRFD ANTYLLMTKA LDYFDPAANF
     NDDLAKTFAN ATARFCVMSF TTDWRFSPAR SRELVDALMA ARKDVCYLEI DAPQGHDAFL
     IPIPRYLQAF GNYMNRISL
 
 
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