SST_SCHPO
ID SST_SCHPO Reviewed; 504 AA.
AC Q10341;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=cys2 {ECO:0000303|PubMed:17622533};
GN ORFNames=SPBC106.17c {ECO:0000312|PomBase:SPBC106.17c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PATHWAY, AND MUTAGENESIS OF GLY-426.
RX PubMed=17622533; DOI=10.1007/s00294-007-0142-1;
RA Ma Y., Sugiura R., Saito M., Koike A., Sio S.O., Fujita Y., Takegawa K.,
RA Kuno T.;
RT "Six new amino acid-auxotrophic markers for targeted gene integration and
RT disruption in fission yeast.";
RL Curr. Genet. 52:97-105(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for L-serine {ECO:0000269|PubMed:28581482};
CC KM=0.025 mM for succinyl-CoA {ECO:0000269|PubMed:28581482};
CC KM=0.045 mM for acetyl-CoA {ECO:0000269|PubMed:28581482};
CC KM=738 mM for L-homoserine {ECO:0000269|PubMed:28581482};
CC Note=kcat is 7.4 sec(-1) with L-serine and succinyl-CoA as
CC substrates. kcat is 0.2 sec(-1) with acetyl-CoA as substrate (in the
CC presence of L-serine). kcat is 13.8 sec(-1) with L-homoserine as
CC substrate (in the presence of succinyl-CoA).
CC {ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000305|PubMed:17622533,
CC ECO:0000305|PubMed:28581482}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB53733.1; -; Genomic_DNA.
DR PIR; T37984; T37984.
DR RefSeq; NP_595166.1; NM_001021075.2.
DR AlphaFoldDB; Q10341; -.
DR SMR; Q10341; -.
DR BioGRID; 276451; 1.
DR STRING; 4896.SPBC106.17c.1; -.
DR ESTHER; schpo-yblh; Homoserine_transacetylase.
DR MaxQB; Q10341; -.
DR PaxDb; Q10341; -.
DR EnsemblFungi; SPBC106.17c.1; SPBC106.17c.1:pep; SPBC106.17c.
DR GeneID; 2539905; -.
DR KEGG; spo:SPBC106.17c; -.
DR PomBase; SPBC106.17c; cys2.
DR VEuPathDB; FungiDB:SPBC106.17c; -.
DR eggNOG; ENOG502QR3J; Eukaryota.
DR HOGENOM; CLU_028760_7_0_1; -.
DR InParanoid; Q10341; -.
DR OMA; NPQPGWW; -.
DR PhylomeDB; Q10341; -.
DR UniPathway; UPA00136; UER00199.
DR PRO; PR:Q10341; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; TAS:PomBase.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IMP:PomBase.
DR GO; GO:0019344; P:cysteine biosynthetic process; IMP:PomBase.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IMP:PomBase.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006555; P:methionine metabolic process; NAS:PomBase.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
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 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; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..504
FT /note="Serine O-succinyltransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000155759"
FT DOMAIN 117..395
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 49..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..127
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:28581482"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 443
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 480
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT SITE 258
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000305|PubMed:28581482"
FT MUTAGEN 426
FT /note="G->D: In cys2-1: Leads to auxotrophy for cysteine."
FT /evidence="ECO:0000269|PubMed:17622533"
SQ SEQUENCE 504 AA; 56363 MW; 1A8C6C9C658392C7 CRC64;
MLRASSKRLQ LSWQVFRRFQ SSNPQLSFPC VDQAQERSRQ FEQSLQKQQA CPNSVDPSAS
ITSPSLSSGP EPVYGKIVSG FKKFYHNKPF LCDHGGILPK FEIAYETWGT LNKDHSNAIL
LHTGLSASSH AHSHPENTAP GWWEQFIGPG KDVDTNKFFV ICTNVLGSCY GSTGPSSVDP
GDGKHYATRF PIITVNDMIR AQLLLLDHLK IEKLYASVGS SLGGMQSLTL GALAPHRVGR
IASISGGARS HPYSIALRFT QRQILMNDPY WNRGFYYDGV PPHTGMKLAR EVATISYRSG
PEWEQRFGNR RADPSVSPAF CPDFLIETYL DHAGEKFCLQ YDPNSLLYIS KAMDMHDMSA
SHQRSLSENR KKNQHKLDKY LSADVSAEEI IKLNEDTSVL PDVPYQEIAN EDRAPEPDPE
TNLIAGLAPL KDTPVMVMGV ESDNLMPVEC QRETARCLEK AGNKQVVYHE LDANESFYGH
DTFLIYRKDL DLVGGKLKKF LELS
