SST_XYLFM
ID SST_XYLFM Reviewed; 370 AA.
AC B0U3V7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Xfasm12_1627;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
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; CP000941; ACA12536.1; -; Genomic_DNA.
DR RefSeq; WP_004086016.1; NC_010513.1.
DR AlphaFoldDB; B0U3V7; -.
DR SMR; B0U3V7; -.
DR ESTHER; xylfa-metx; Homoserine_transacetylase.
DR KEGG; xfm:Xfasm12_1627; -.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
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..370
FT /note="Serine O-succinyltransferase"
FT /id="PRO_1000115239"
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; 40875 MW; 54131D11D311A3E3 CRC64;
MTEFIPPGSL FHALSSPFAM KRGGQLHHAR IAYETWGRLN ASATNAILIM PGLSPNAHAA
HHDSNAEPGW WESMLGPGKP IDTDRWFVIC VNSLGSCKGS TGPASYNPIT QAMYRLDFPA
LSIEDGANSA IEVVHALGIK QLASLIGNSM GGMTALAILL LHPDIARSHI NISGSAQALP
FSIAIRSLQR EAIRLDPHWR QGDYDDTHYP ESGLRIARKL GVITYRSALE WDGRFGRVRL
DSDQTNDTPF GLEFQIENYL ESHAHRFVHT FDPNCYLYLS RSMDWFDVAE YANGDILAGL
ARIRIQRALA IGSHTDILFP IQQQQQIAEG LRRGGTHATF LGLDSPQGHD AFLVDIARFG
PPVKEFLDEL
