ID A0A1I1Y5Y4_9GAMM Unreviewed; 368 AA.
AC A0A1I1Y5Y4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Serine O-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
DE Short=SST {ECO:0000256|HAMAP-Rule:MF_00296};
DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_00296};
GN ORFNames=SAMN02799615_00500 {ECO:0000313|EMBL:SFE14839.1};
OS Dyella marensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=500610 {ECO:0000313|EMBL:SFE14839.1, ECO:0000313|Proteomes:UP000199477};
RN [1] {ECO:0000313|EMBL:SFE14839.1, ECO:0000313|Proteomes:UP000199477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC178MFTsu3.1 {ECO:0000313|EMBL:SFE14839.1,
RC ECO:0000313|Proteomes:UP000199477};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-serine,
CC forming succinyl-L-serine. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00296};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR EMBL; FONH01000001; SFE14839.1; -; Genomic_DNA.
DR RefSeq; WP_026634506.1; NZ_FONH01000001.1.
DR AlphaFoldDB; A0A1I1Y5Y4; -.
DR STRING; 500610.SAMN02799615_00500; -.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000199477; Unassembled WGS sequence.
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; 1.10.1740.110; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 44..352
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 49..52
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 314
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 347
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT SITE 183
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 368 AA; 40272 MW; A45FECF97E9B144D CRC64;
MSHDARRYFS LPSPFPMKRG GELHGARVAF ETWGALSDAR DNALLILTGL SPSAHAASNE
QDPSPGWWEA MIGPGKAIDT DRWFVICVNS LGSDKGSTCP ASIDPATGEP YRLSFPELAL
EDVANAAHAA VSSLGIEQLA CLVGCSMGGM SALAYMLLHP GSVRTHISVD TAPQAQPFAI
AIRSLQREAI RLDPQWNNGR YDDAHYPETG MSIARKLGVI TYRSAMEWNG RFARIRLDAE
QRDDDVPFGF EFQVESYLEG HAQRFVRTFD PNSYLYLSRA SDWFDISEYG EGSIQAGLKR
IRVEQALVIG VSTDILFPLE QQEQIAEGLE AAGAAVEFVA LDSPQGHDAF LVDIENYSRA
IGGFLGRL
//
