ID   CYSKL_SCHPO             Reviewed;         395 AA.
AC   P87131;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Cysteine synthase 2 {ECO:0000305|PubMed:14981292};
DE            Short=CS 2;
DE            EC=2.5.1.47;
DE   AltName: Full=Cysteine synthase-like protein {ECO:0000303|PubMed:17482430};
DE            Short=CSl;
DE   AltName: Full=O-acetylserine (thiol)-lyase 2;
DE            Short=OAS-TL 2;
DE   AltName: Full=O-acetylserine sulfhydrylase 2;
GN   Name=cys12; Synonyms=cys1b {ECO:0000303|PubMed:14981292};
GN   ORFNames=SPAC3A12.17c {ECO:0000312|PomBase:SPAC3A12.17c};
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   FUNCTION.
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.
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).
CC   -!- FUNCTION: Putative cysteine synthase that catalyzes the conversion of
CC       O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine
CC       biosynthesis pathway. However, in contrast to cysteine synthase cys11,
CC       this CS-like protein does not seem to function in cysteine
CC       biosynthesis, at least under normal growth conditions, although the
CC       transcript is produced. {ECO:0000269|PubMed:14981292,
CC       ECO:0000305|PubMed:17482430}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate;
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:0000250|UniProtKB:P0ABK5};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC       Mitochondrion outer membrane {ECO:0000250|UniProtKB:P53206}; Single-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB08745.1; -; Genomic_DNA.
DR   PIR; T38685; T38685.
DR   RefSeq; NP_593343.1; NM_001018775.3.
DR   AlphaFoldDB; P87131; -.
DR   SMR; P87131; -.
DR   BioGRID; 279038; 1.
DR   FunCoup; P87131; 353.
DR   STRING; 284812.P87131; -.
DR   iPTMnet; P87131; -.
DR   PaxDb; 284812-P87131; -.
DR   GeneID; 2542583; -.
DR   KEGG; spo:2542583; -.
DR   PomBase; SPAC3A12.17c; cys12.
DR   VEuPathDB; FungiDB:SPAC3A12.17c; -.
DR   eggNOG; KOG1481; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   InParanoid; P87131; -.
DR   OMA; WMADYGF; -.
DR   PhylomeDB; P87131; -.
DR   PRO; PR:P87131; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004124; F:cysteine synthase activity; ISS:UniProtKB.
DR   CDD; cd01561; CBS_like; 1.
DR   FunFam; 3.40.50.1100:FF:000096; Related to cysteine synthase; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Cysteine synthase 2"
FT                   /id="PRO_0000167129"
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         228..232
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P16703"
FT   BINDING         335
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P16703"
FT   MOD_RES         83
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16703"
SQ   SEQUENCE   395 AA;  43086 MW;  94C3096B7761A64D CRC64;
     MAKKYQDLAS GIAMGAVFMY LLRRLYESLR VKSSADSLEE DIVNGVEGLI GNTKMVRIKS
     LSQATGCDIL AKAEFLNPGN SPKDRVALQM IRTAEENGDL VPYQSNAVYE GTAGSTGISI
     AMLCCSLGYD SRIYMPSDQS KEKSDILELL GAHVQRVTPA PIVDPNHFVN TARRNAANHT
     VDESIPGKGY FANQFENPAN WQAHFNSTGP EIWRQCAGKL DAFIAGSGTG GTIAGISRYL
     KSKDPSITVC LADPPGSGLY HKVLHGVMFD LAEREGTRRR HQVDTIVEGV GINRMTRNFS
     IAEPLIDMAY RVTDEQAVAM SRYLVTHDGL FVGSSSAVNC VAAVRLAKKL GPGHRIVTLL
     CDPGSRHFSK LYNEEFLRKK NIVPQVPSSL DFVEA
//