ID   SST_EMEND               Reviewed;         517 AA.
AC   A0A1D3PCM3;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Serine O-succinyltransferase {ECO:0000305};
DE            Short=SST {ECO:0000303|PubMed:28581482};
DE            EC=2.3.1.- {ECO:0000269|PubMed:28581482};
DE   Flags: Precursor;
GN   Name=CysA {ECO:0000312|EMBL:SCN13867.1};
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ATCC 11267 / DSM 820;
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. Has also weak serine acetyl transferase
CC       activity and homoserine succinyl transferase activity.
CC       {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;
CC         Evidence={ECO:0000269|PubMed:28581482};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 1/2. {ECO:0000305|PubMed:28581482}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q10341}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000305}.
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DR   EMBL; LT613643; SCN13867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D3PCM3; -.
DR   SMR; A0A1D3PCM3; -.
DR   ESTHER; emeni-CYSC; Homoserine_transacetylase.
DR   UniPathway; UPA00136; UER00199.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
KW   Mitochondrion; Transferase; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..517
FT                   /note="Serine O-succinyltransferase"
FT                   /id="PRO_0000441641"
FT   DOMAIN          134..386
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          34..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..144
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000305|PubMed:28581482"
FT   REGION          413..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        238
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P45131"
FT   ACT_SITE        461
FT                   /evidence="ECO:0000250|UniProtKB:P45131"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000250|UniProtKB:P45131"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45131"
FT   BINDING         499
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45131"
FT   SITE            275
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000305|PubMed:28581482"
SQ   SEQUENCE   517 AA;  56389 MW;  DCCBA610AF6F87FA CRC64;
     MSPLNGVARS LPRPFQAVAR RPFRVAQPAV ACPSNRRSFN HSRSLRSTGS QSPAPSPRDS
     SNPALSFPCL DAQEAKSALL SARSLGSGPE PSYTAGHHER FHSDEPLLLD WGGLLPEFDI
     AYETWGQLNE KKDNVILLHT GLSASSHAHS TEANPKPGWW EKFIGPGKTL DTDKYFVICT
     NVLGGCYGST GPSTVDPSDG KKYATRFPIL TIEDMVRAQF RLLDHLGVRK LYASVGSSMG
     GMQSLAAGVL FPERVGKIVS ISGCARSHPY SIAMRHTQRQ VLMMDPNWAR GFYYDSIPPH
     SGMKLAREIA TVTYRSGPEW EKRFGRKRAD PSKQPALCPD FLIETYLDHA GEKFCLEYDA
     NSLLYISKAM DLFDLGLTQQ LATKKQRAEA QAKISSGTNT VNDASCSLTL PEQPYQEQPS
     ASTSAEQSAS ASETGSAPND LVAGLAPLKD HQVLVIGVAS DILFPAWQQR EIAETLIQAG
     NKTVEHIELG NDVSLFGHDT FLLDVKNVGG AVRKFLD