ID   METAS_SHIB3             Reviewed;         309 AA.
AC   B2TWJ5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HST {ECO:0000255|HAMAP-Rule:MF_00295};
DE            EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00295};
DE   AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00295};
DE            Short=HTS {ECO:0000255|HAMAP-Rule:MF_00295};
GN   Name=metAS {ECO:0000255|HAMAP-Rule:MF_00295};
GN   OrderedLocusNames=SbBS512_E4507;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC       forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00295}.
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_00295};
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_00295}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295}.
CC   -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00295}.
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DR   EMBL; CP001063; ACD07330.1; -; Genomic_DNA.
DR   RefSeq; WP_001122787.1; NC_010658.1.
DR   AlphaFoldDB; B2TWJ5; -.
DR   SMR; B2TWJ5; -.
DR   STRING; 344609.SbBS512_E4507; -.
DR   EnsemblBacteria; ACD07330; ACD07330; SbBS512_E4507.
DR   KEGG; sbc:SbBS512_E4507; -.
DR   HOGENOM; CLU_057851_0_1_6; -.
DR   OMA; WLWFCYQ; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000001030; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR   CDD; cd03131; GATase1_HTS; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00295; MetA_acyltransf; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005697; HST_MetA.
DR   InterPro; IPR033752; MetA_family.
DR   PANTHER; PTHR20919; PTHR20919; 1.
DR   Pfam; PF04204; HTS; 1.
DR   PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01001; metA; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Methionine biosynthesis; Transferase.
FT   CHAIN           1..309
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_1000115196"
FT   ACT_SITE        142
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            111
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT   SITE            192
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
SQ   SEQUENCE   309 AA;  35757 MW;  E2C0AC89B4AFF065 CRC64;
     MPIRVPDELP AVNFLREENV FVMTTSRASG QEIRPLKVLI LNLMPKKIET ENQFLRLLSN
     SPLQVDIQLL RIDSRESRNT PAEHLNNFYC NFEDIQEQNF DGLIVTGAPL GLVEFNDVAY
     WPQIKQVLEW SKDHVTSTLF VCWAVQAALN ILYGIPKQTR TDKLSGVYEH HILHPHALLT
     RGFDDSFLAP HSRYADFPAA LIRDYTDLEI LAETEEGDAY LFASKDKRIA FVTGHPEYDA
     QTLAQEYFRD VEAGLDPEVP YNYFPHNDPQ NTPRASWRSH GNLLFTNWLN YYVYQITPYD
     LRHMNPTLD