CYSK_SCHPO
ID CYSK_SCHPO Reviewed; 351 AA.
AC O59701;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cysteine synthase 1 {ECO:0000305|PubMed:14981292};
DE Short=CS 1;
DE EC=2.5.1.- {ECO:0000269|PubMed:28581482};
DE EC=2.5.1.47 {ECO:0000269|PubMed:17482430, ECO:0000269|PubMed:28581482};
DE AltName: Full=O-acetylserine (thiol)-lyase 1;
DE Short=OAS-TL 1;
DE AltName: Full=O-acetylserine sulfhydrylase 1;
DE AltName: Full=O-succinylserine sulfhydrylase {ECO:0000305};
DE Flags: Precursor;
GN Name=cys11; Synonyms=cys1a {ECO:0000303|PubMed:14981292};
GN ORFNames=SPBC36.04 {ECO:0000312|PomBase:SPBC36.04};
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 PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 38399;
RX PubMed=14981292; DOI=10.1271/bbb.68.306;
RA Fujita Y., Takegawa K.;
RT "Characterization of two genes encoding putative cysteine synthase required
RT for cysteine biosynthesis in Schizosaccharomyces pombe.";
RL Biosci. Biotechnol. Biochem. 68:306-311(2004).
RN [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17482430; DOI=10.1016/j.resmic.2007.03.002;
RA Brzywczy J., Natorff R., Sienko M., Paszewski A.;
RT "Multiple fungal enzymes possess cysteine synthase activity in vitro.";
RL Res. Microbiol. 158:428-436(2007).
RN [5]
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: Catalyzes the conversion of O-succinyl-L-serine into
CC cysteine, the last step in the cysteine biosynthesis pathway
CC (PubMed:28581482). Can also use O-acetyl-L-serine (PubMed:17482430,
CC PubMed:28581482). {ECO:0000269|PubMed:28581482,
CC ECO:0000305|PubMed:17482430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-succinyl-L-serine = L-cysteine +
CC succinate; Xref=Rhea:RHEA:53816, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:136856;
CC Evidence={ECO:0000269|PubMed:28581482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000269|PubMed:17482430, ECO:0000269|PubMed:28581482};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for O-succinyl-L-serine {ECO:0000269|PubMed:28581482};
CC KM=0.33 mM for O-acetyl-L-serine {ECO:0000269|PubMed:28581482};
CC KM=0.34 mM for Na(2)S {ECO:0000269|PubMed:28581482};
CC Note=kcat is 2.8 sec(-1) with O-succinyl-L-serine as substrate. kcat
CC is 1.5 sec(-1) with O-acetyl-L-serine as substrate.
CC {ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000305|PubMed:14981292,
CC ECO:0000305|PubMed:28581482}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14981292}.
CC -!- DISRUPTION PHENOTYPE: Causes cysteine auxotrophy.
CC {ECO:0000269|PubMed:14981292}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19052.1; -; Genomic_DNA.
DR PIR; T40299; T40299.
DR RefSeq; NP_595332.1; NM_001021240.2.
DR AlphaFoldDB; O59701; -.
DR SMR; O59701; -.
DR BioGRID; 277462; 55.
DR STRING; 4896.SPBC36.04.1; -.
DR iPTMnet; O59701; -.
DR MaxQB; O59701; -.
DR PaxDb; O59701; -.
DR PRIDE; O59701; -.
DR EnsemblFungi; SPBC36.04.1; SPBC36.04.1:pep; SPBC36.04.
DR GeneID; 2540946; -.
DR KEGG; spo:SPBC36.04; -.
DR PomBase; SPBC36.04; cys11.
DR VEuPathDB; FungiDB:SPBC36.04; -.
DR eggNOG; KOG1481; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; O59701; -.
DR OMA; WMADYGF; -.
DR PhylomeDB; O59701; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:O59701; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004124; F:cysteine synthase activity; IMP:PomBase.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IMP:PomBase.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..351
FT /note="Cysteine synthase 1"
FT /id="PRO_0000167128"
FT BINDING 84
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 190..194
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 289
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P16703"
SQ SEQUENCE 351 AA; 37853 MW; EF11655CE2BE4A60 CRC64;
MATSGIQTKV PGIVSGFIGA IGRTPLIRLN TLSNETGCNI LAKAEFQNPG GSVKDRAAYY
VVRDAEKKGK LSRGGTIVEG TAGNTGIGLA HIARARGYKC VIYMPNTQSQ AKIDTLKFLG
AEVHPVPVAP FSNPLNYNHQ ARRHAESTPN ASWTDQFDNV ANLLSHYETT GPEIWDQTKG
TVDGFTCSTG TGGTFAGVTK YLKEKSDGRV ASFVADPPGS VLYSHIKTKG KHPDNKGSSF
TEGIGQGRIT GNVQPVYDLI DDAMKIPDEK SINMFFRLLD QEGLFLGGSS CLNVVAAVEM
AKILGPGKTV VTILCDSGHK YATRLFSRSF LESKKLFDVI EPQYKKYIVL P
