ID   SST_STRMK               Reviewed;         370 AA.
AC   B2FMC1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Smlt3277;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(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; AM743169; CAQ46716.1; -; Genomic_DNA.
DR   RefSeq; WP_005413993.1; NC_010943.1.
DR   AlphaFoldDB; B2FMC1; -.
DR   SMR; B2FMC1; -.
DR   STRING; 522373.Smlt3277; -.
DR   ESTHER; strmk-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; CAQ46716; CAQ46716; Smlt3277.
DR   KEGG; sml:Smlt3277; -.
DR   PATRIC; fig|522373.3.peg.3075; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_6; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000008840; 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   Reference proteome; Transferase.
FT   CHAIN           1..370
FT                   /note="Serine O-succinyltransferase"
FT                   /id="PRO_1000115236"
FT   DOMAIN          46..355
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        316
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         350
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   370 AA;  40012 MW;  0F38E593B298F15A CRC64;
     MTEFIPPGTR FHALPSPFPF KRGGALHGAR VAYETWGTLA ADASNAILIV TGLSPDAHAA
     ANDANPAAGW WEGMVGPGKA IDTDRWFVVC VNSLGSCKGS TGPASLNPAT GQPYRLDFPE
     LSIEDGARAA IEVVRALGIE QLACVVGNSM GGMTALAVLM LHPGIARSHV NISGSAQALP
     FSIAIRSLQR EAIRLDPRWN GGHYDDDAYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
     DSDQTDDDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE YADGDVLAGL
     AKIRVEKALA IGANTDILFP VQQQQQVADG LRAGGADAHF IGLESPQGHD AFLVDFDRFG
     PAVRGFLDAL