ID   METXS_HALAF             Reviewed;         390 AA.
AC   S2L5R8;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 48.
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};
GN   ORFNames=L861_08120 {ECO:0000312|EMBL:EPC00121.1};
OS   Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1121939;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35;
RX   PubMed=23868129; DOI=10.1128/genomea.00497-13;
RA   Tahrioui A., Quesada E., Llamas I.;
RT   "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT   Halomonas anticariensis FP35.";
RL   Genome Announc. 1:31-31(2013).
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 a succinyl group from succinyl-CoA to L-homoserine,
CC       forming succinyl-L-homoserine. In vitro, has also serine succinyl
CC       transferase activity. {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   -!- 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; ASTJ01000044; EPC00121.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2L5R8; -.
DR   SMR; S2L5R8; -.
DR   STRING; 1121939.L861_08120; -.
DR   EnsemblBacteria; EPC00121; EPC00121; L861_08120.
DR   PATRIC; fig|1121939.11.peg.4562; -.
DR   eggNOG; COG2021; Bacteria.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000014463; Unassembled WGS sequence.
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; Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_0000440302"
FT   DOMAIN          56..365
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        162
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            329
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT                   ECO:0000305|PubMed:28581482"
SQ   SEQUENCE   390 AA;  42772 MW;  81E2F140B6BA8BDD CRC64;
     MDSDTLMPEL PSDSVGLVAP QTAHFDVPLA LACGKTLQSY DLVYETYGKL NASRSNAVLI
     CHALSGHHHA AGYHSREDRK PGWWDAHIGP GKSIDTDRFF VISLNNLGGC HGSTGPCAIN
     PDTGRQWGPD FPMMTVGDWV HSQARLADRL GIERFAAVIG GSLGGMQVLQ WSLAYPERIA
     NAVVIAATPK LSAQNIAFNE VARQAIRSDP DFYDGWYAEH DTLPRRGLKL ARMVGHITYL
     SEDAMGSKFG RDLRSDDLNF GYDVEFQVES YLRYQGDTFS TSFDANTYLL MTKALDYFDP
     AAAHDGDLAA AVAPASCPFL VVSFSTDWRF PPSRSRELVD ALIRAGKPVS YVCIDSPHGH
     DAFLLPETRY QAIFASFMGR VAHDSGLEDS