SST_STEMA
ID SST_STEMA Reviewed; 370 AA.
AC A0A0I9RJ56;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Serine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
DE Short=SST {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine O-succinyltransferase {ECO:0000305};
DE Short=HST {ECO:0000303|PubMed:28581482};
DE EC=2.3.1.46 {ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000305};
DE Short=HTS {ECO:0000305};
OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS maltophilia).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=40324;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=DSM 50170;
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-serine,
CC forming succinyl-L-serine. In vitro, has also homoserine succinyl
CC transferase activity. {ECO:0000269|PubMed:28581482}.
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, ECO:0000269|PubMed:28581482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine;
CC Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46;
CC Evidence={ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000305|PubMed:28581482}.
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; LN871226; CTQ31229.1; -; Genomic_DNA.
DR EMBL; MTGD01000005; OOD19792.1; -; Genomic_DNA.
DR RefSeq; WP_024958402.1; NZ_MTGD01000005.1.
DR AlphaFoldDB; A0A0I9RJ56; -.
DR SMR; A0A0I9RJ56; -.
DR STRING; 1429851.X548_12020; -.
DR EnsemblBacteria; OOD19792; OOD19792; BWP19_01985.
DR PATRIC; fig|40324.61.peg.524; -.
DR eggNOG; COG2021; Bacteria.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000189183; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Transferase.
FT CHAIN 1..370
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000440309"
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 ECO:0000305|PubMed:28581482"
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,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 370 AA; 40134 MW; 525B68B8784CC171 CRC64;
MTEFIPPGTR FHALPSPFPF KRGGALHGAR VAYETWGTLA ADASNAILIV TGLSPDAHAA
ANDANPAAGW WEGMVGPGKA IDTDRWFVVC VNSLGSCRGS TGPASLNPAT GQPYRLDFPE
LSIEDGARAA IEVVRAQGIE QLACVVGNSM GGMTALAVLM LHPGIARSHV NISGSAQALP
FSIAIRSLQR EAIRLDPRWN GGHYDDDAYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
DSDQTDDDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE YADGDVLAGL
AKIRVEKALA IGANTDILFP VQQQQQVADG LRAGGADARF IGLESPQGHD AFLVDFERFC
PAVRGFLDAL
