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SST_XYLF2
ID   SST_XYLF2               Reviewed;         370 AA.
AC   B2I700;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=XfasM23_1569;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB92977.1; -; Genomic_DNA.
DR   RefSeq; WP_004088494.1; NC_010577.1.
DR   AlphaFoldDB; B2I700; -.
DR   SMR; B2I700; -.
DR   ESTHER; xylfa-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ACB92977; ACB92977; XfasM23_1569.
DR   GeneID; 58017007; -.
DR   KEGG; xfn:XfasM23_1569; -.
DR   HOGENOM; CLU_028760_1_2_6; -.
DR   OMA; TRFCVVS; -.
DR   UniPathway; UPA00136; UER00199.
DR   Proteomes; UP000001698; 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..370
FT                   /note="Serine O-succinyltransferase"
FT                   /id="PRO_1000115238"
FT   DOMAIN          45..354
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;  40724 MW;  37464809AA96FBFD CRC64;
     MTEFIPPGSL FHALSSPFAM KRGGQLHHAR IAYETWGRLN AGATNAILIM PGLSPNAHAA
     HHDSNAEPGW WESMLGPGKP IDTDRWFVIC VNSLGSCKGS TGPASYNPIT QAMYRLDFPA
     LSIEDGANAA IEVVHALGIK QLASLIGNSM GGMTALAILL LHPDIARSHI NISGSAQALP
     FSIAIRSLQR EAIRLDPHWK QGHYDDTHYP ESGLRIARKL GVITYRSALE WDGRFGRVRL
     DSDQTNDTPF GLEFQIENYL ESHAHRFVHT FDPNCYLYLS RSMDWFDVAE YANGDIIAGL
     ARIRIQRALA IGSHTDILFP IQQQQQIAEG LRRGGTHATF LGLDSPQGHD AFLVDIAGFG
     PPVKEFLDEL
 
 
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