SST_XANC5
ID SST_XANC5 Reviewed; 400 AA.
AC Q3BSK1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=XCV2531;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(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; AM039952; CAJ24208.1; -; Genomic_DNA.
DR RefSeq; WP_011347689.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BSK1; -.
DR SMR; Q3BSK1; -.
DR STRING; 456327.BJD11_10250; -.
DR ESTHER; xanax-METX; Homoserine_transacetylase.
DR EnsemblBacteria; CAJ24208; CAJ24208; XCV2531.
DR KEGG; xcv:XCV2531; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000007069; 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; -; 2.
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..400
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000231890"
FT DOMAIN 45..385
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 346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 380
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 400 AA; 43111 MW; B2F8F8380CD65B38 CRC64;
MTEFIPAGTL YHALPSPFPM KRGGVLHQAR VAYETWGTLA ADRSNAILIV TGLSPNAHAA
ANQANPEPGW WEAMLGPGKP IDTARWFVVC VNSLGSCKGS TGPASVNPAT GAPYRLSFPD
LSIEDVADAA ADVVRALGIA QLACLIGNSM GGMTALALLL RHPGIARSHI NISGSAQALP
FSIAIRSLQR EAIRLDPHWN GGHYDDARYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
DSEQAADDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE HVDEQPATDS
AIDHAHADAL PASAKPQTGV STADTVLAGL ARIRIARALA IGANTDILFP VQQQEQIADG
LRAGGADAHF IGLDSPQGHD AFLVDFARFG PAVRDFLQDC