ID   SST_XANCB               Reviewed;         380 AA.
AC   B0RS70;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Serine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE            Short=SST {ECO:0000255|HAMAP-Rule:MF_00296};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00296};
GN   Name=metX; OrderedLocusNames=xcc-b100_1952;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-serine,
CC       forming succinyl-L-serine. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine + succinyl-CoA = CoA + O-succinyl-L-serine;
CC         Xref=Rhea:RHEA:52820, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:136856; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00296};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2. {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; AM920689; CAP51305.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RS70; -.
DR   SMR; B0RS70; -.
DR   ESTHER; xanca-METX; Homoserine_transacetylase.
DR   KEGG; xca:xcc-b100_1952; -.
DR   HOGENOM; CLU_028760_1_2_6; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016750; F:O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; 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; Cysteine biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..380
FT                   /note="Serine O-succinyltransferase"
FT                   /id="PRO_1000115237"
FT   DOMAIN          45..365
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   REGION          52..55
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        149
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        359
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            186
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   380 AA;  41031 MW;  9FEBCC885EDD6527 CRC64;
     MTEFIPTGTR FHALPSPLPM KRGGVLHQAR VAYETWGTLD ADHGNAVLIV TGLSPNAHAA
     ANADNPEPGW WEAMVGPGKP IDTDRWFVVC VNSLGSCKGS TGPASIDPAT GAPYRLSFPE
     LSIEDVADAA ADVVRALGIA QLACLIGNSM GGMTALALLL RHPGIARSHI NISGSAQALP
     FSIAIRSLQR EAIRLDPHWN GGHYDDVQYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
     DSELTAEDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE YAPDTRADAA
     APESGVLAGL AQIRIARALA IGANTDILFP VQQQEQIAEG LRAGGADAQF LGLDSPQGHD
     AFLVDFARFG PAVRAFLADC