SST_HALAF
ID SST_HALAF Reviewed; 367 AA.
AC S2KHP1;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 46.
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 ORFNames=L861_05420 {ECO:0000312|EMBL:EPC01480.1};
OS Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121939;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35;
RX PubMed=23868129; DOI=10.1128/genomea.00497-13;
RA Tahrioui A., Quesada E., Llamas I.;
RT "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT Halomonas anticariensis FP35.";
RL Genome Announc. 1:31-31(2013).
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}.
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DR EMBL; ASTJ01000035; EPC01480.1; -; Genomic_DNA.
DR RefSeq; WP_016417653.1; NZ_KE386756.1.
DR AlphaFoldDB; S2KHP1; -.
DR SMR; S2KHP1; -.
DR STRING; 1121939.L861_05420; -.
DR EnsemblBacteria; EPC01480; EPC01480; L861_05420.
DR PATRIC; fig|1121939.11.peg.3135; -.
DR eggNOG; COG2021; Bacteria.
DR OMA; WDQARSI; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000014463; 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 Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000440308"
FT DOMAIN 41..349
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 145
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 345
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 182
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 367 AA; 39929 MW; 3887BDB3FF174452 CRC64;
MPDARRFIEL PGPVRMYRGG ELPSVTIAYE TWGELRGQGD NALLLFTGLS PSAHAASSMA
DPSPGWWEYM IGPGKPIDTE RFFVIAINSL GSCFGSTGPA SINPATGQPY RLDFPKLSVE
DIVAAARGAC RALGIDHVHT VAGASLGGMD ALAYAVMYPG TYRDIISISA AAHATPFTIA
LRSIQREAVR ADPAWAGGNY APGEGPKDGM RVARQLGILT YRSAEEWLQR FDRERLEGSD
DSANPFAMAF QVQSYMEANA RKFADRFDAN CYLYLSQAMD LFDMAEHGDG SLEAAVRRID
AKRALVAGVT TDWLFPLWQQ RQVAELLEHA GVAVSYHELG SIQGHDAFLV DSERFAPMVA
EFLAHSS
