SST_FRAAD
ID SST_FRAAD Reviewed; 367 AA.
AC H8L374;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
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};
GN OrderedLocusNames=Fraau_1049 {ECO:0000312|EMBL:AFC85510.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 / NCIMB
RC 13370;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003350; AFC85510.1; -; Genomic_DNA.
DR RefSeq; WP_014402516.1; NC_017033.1.
DR AlphaFoldDB; H8L374; -.
DR SMR; H8L374; -.
DR STRING; 767434.Fraau_1049; -.
DR EnsemblBacteria; AFC85510; AFC85510; Fraau_1049.
DR KEGG; fau:Fraau_1049; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000005234; Chromosome.
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 Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000440307"
FT DOMAIN 41..351
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 48..51
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 313
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 183
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 367 AA; 40076 MW; 49235D62ADF8031A CRC64;
MSDARRYHAL PSPFPMKRGG QLQGARLAYE TWGRLSPGCD NAVLILTGLS PSAHAASHPD
GDTSPGWWEG MLGPGKAIDT DRWYVICVNS LGSDKGSTGP ASPDPATGAP YRLSFPELAL
EDVASAAHDL VKALGIARLA CLIGCSMGGM SALAYMLQYE GEVEAHISVD TAPQAQPFAI
AIRSLQREAI RLDPNWQDGH YTDAAYPETG MAMARKLGVI TYRSAMEWNG RFARIRLDGD
QRPDEPFARE FQVESYLEHH AQRFVRRFDP ACYLYLTRAS DWFDVAEYGE GSVMQGLARI
HVRRALVIGV STDILFPLEQ QQQIAEGLQA AGAEVDFVAL DSPQGHDAFL VDIENYSAAI
GGFLRTL
