CYSKL_SCHPO
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 03-AUG-2022, entry version 155.
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 seems not to function in cysteine biosynthesis, at
CC least under normal growth conditions, although the transcript is
CC produced. {ECO:0000269|PubMed:14981292, ECO:0000305|PubMed:17482430}.
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: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_001018775.2.
DR AlphaFoldDB; P87131; -.
DR SMR; P87131; -.
DR BioGRID; 279038; 1.
DR STRING; 4896.SPAC3A12.17c.1; -.
DR MaxQB; P87131; -.
DR PaxDb; P87131; -.
DR EnsemblFungi; SPAC3A12.17c.1; SPAC3A12.17c.1:pep; SPAC3A12.17c.
DR GeneID; 2542583; -.
DR KEGG; spo:SPAC3A12.17c; -.
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; FWDSGER; -.
DR PhylomeDB; P87131; -.
DR PRO; PR:P87131; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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 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
