ID   SST_XANOM               Reviewed;         399 AA.
AC   Q2P3Z2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=XOO1980;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE68735.1; -; Genomic_DNA.
DR   RefSeq; WP_011258800.1; NC_007705.1.
DR   AlphaFoldDB; Q2P3Z2; -.
DR   SMR; Q2P3Z2; -.
DR   ESTHER; xanor-metx; Homoserine_transacetylase.
DR   KEGG; xom:XOO1980; -.
DR   HOGENOM; CLU_028760_1_2_6; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00136; UER00199.
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..399
FT                   /note="Serine O-succinyltransferase"
FT                   /id="PRO_0000231892"
FT   DOMAIN          45..384
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        345
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         379
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   399 AA;  43044 MW;  350B49A02511681F CRC64;
     MTEFIPLGTL YHALPSPFQM KRGGVLHQAH VAYETWGALA ADRSNAVLIV TGLSPNAHAA
     ANQANPEPGW WEAMVGPGKP IDTARWFVVC VNSLGSCKGS TGPASVNPAT GALYRLTFPD
     LSIEDVADAA ADVVRALGIA QLACLIGNSM GGMTALALLL RHPGIARSHI NISGSAQALP
     FSIAIRSLQR EAIRLDPHWN GGHYDDTRYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
     DSEQSEDDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE YVDDKPAADM
     GIDSPGADAL PAAKSETGVS TASTVLAGLA RIRIARALAI GANTDILFPV QQQEQIADGL
     RAGDADARFI GLDSPQGHDA FLVDFARFGP AVRDFLQGC