ID   METXS_DECAR             Reviewed;         374 AA.
AC   Q47JU2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=HST {ECO:0000255|HAMAP-Rule:MF_00296};
DE            EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296};
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}; OrderedLocusNames=Daro_0130;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
CC   -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC       forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}.
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   -!- 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; CP000089; AAZ44889.1; -; Genomic_DNA.
DR   RefSeq; WP_011285899.1; NC_007298.1.
DR   AlphaFoldDB; Q47JU2; -.
DR   SMR; Q47JU2; -.
DR   STRING; 159087.Daro_0130; -.
DR   ESTHER; decar-metx; Homoserine_transacetylase.
DR   PRIDE; Q47JU2; -.
DR   EnsemblBacteria; AAZ44889; AAZ44889; Daro_0130.
DR   KEGG; dar:Daro_0130; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_4; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00075.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Transferase.
FT   CHAIN           1..374
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_0000231869"
FT   DOMAIN          47..357
FT                   /note="AB hydrolase-1"
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        318
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            320
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   374 AA;  41191 MW;  383091CAE410EAD5 CRC64;
     MPGQSVGAVQ PQRAHFDQPL HLRSGGVLPA YDLVYETYGT LNAAKSNAIL VCHALSGHHH
     VAGHYADQPD NIGWWDNIVG PGRPLDTDKF FIVGLNNLGG CHGSTGPSSL NPATGKPWGA
     DFPIVAVNDW VHAQARLADL LGIDSWAAVM GGSLGGMQAL RWSITFPERV RNAIVIAAAP
     KLSAQNIAFN DVARQAILTD PDFHGGHYYE HNTRPVRGLR LARMLGHITY LSDDQMGEKF
     GRELRNSAFS FGYGVEFEVE SYLRYQGDKF AGYFDANTYL LMTKALDYFD PSREDDGNLT
     ATMARTQANF LIASFTTDWR FTPARSKEIV AALLANGRNV SYAEIDLNFG HDSFLMEDAH
     YHGVVDAYLR NIKL