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Protein

Cysteine synthase 1

Gene

cys11

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway.1 Publication1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.By similarity

Cofactori

pyridoxal 5'-phosphateBy similarity

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable serine-O-acetyltransferase (cys2), Putative serine acetyltransferase (SPAC1039.08)
  2. Cysteine synthase 1 (cys11)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Pyridoxal phosphateBy similarity
Binding sitei289 – 2891Pyridoxal phosphateBy similarity

GO - Molecular functioni

  • cysteine synthase activity Source: PomBase
  • pyridoxal phosphate binding Source: GO_Central
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • cysteine biosynthetic process from serine Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1819-MONOMER.
ReactomeiR-SPO-1614603. Cysteine formation from homocysteine.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase 11 Publication (EC:2.5.1.47)
Short name:
CS 1
Alternative name(s):
O-acetylserine (thiol)-lyase 1
Short name:
OAS-TL 1
O-acetylserine sulfhydrylase 1
Gene namesi
Name:cys11
Synonyms:cys1a1 Publication
ORF Names:SPBC36.04Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC36.04.
PomBaseiSPBC36.04. cys11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Causes cysteine auxotrophy.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 351322Cysteine synthase 1PRO_0000167128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiO59701.

Interactioni

Protein-protein interaction databases

BioGridi277462. 50 interactions.
MINTiMINT-4675483.

Structurei

3D structure databases

ProteinModelPortaliO59701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1945Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000217393.
InParanoidiO59701.
KOiK01738.
OMAiEDTHAEM.
OrthoDBiEOG77DJGD.
PhylomeDBiO59701.

Family and domain databases

InterProiIPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSGIQTKV PGIVSGFIGA IGRTPLIRLN TLSNETGCNI LAKAEFQNPG
60 70 80 90 100
GSVKDRAAYY VVRDAEKKGK LSRGGTIVEG TAGNTGIGLA HIARARGYKC
110 120 130 140 150
VIYMPNTQSQ AKIDTLKFLG AEVHPVPVAP FSNPLNYNHQ ARRHAESTPN
160 170 180 190 200
ASWTDQFDNV ANLLSHYETT GPEIWDQTKG TVDGFTCSTG TGGTFAGVTK
210 220 230 240 250
YLKEKSDGRV ASFVADPPGS VLYSHIKTKG KHPDNKGSSF TEGIGQGRIT
260 270 280 290 300
GNVQPVYDLI DDAMKIPDEK SINMFFRLLD QEGLFLGGSS CLNVVAAVEM
310 320 330 340 350
AKILGPGKTV VTILCDSGHK YATRLFSRSF LESKKLFDVI EPQYKKYIVL

P
Length:351
Mass (Da):37,853
Last modified:August 1, 1998 - v1
Checksum:iEF11655CE2BE4A60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19052.1.
PIRiT40299.
RefSeqiNP_595332.1. NM_001021240.2.

Genome annotation databases

EnsemblFungiiSPBC36.04.1; SPBC36.04.1:pep; SPBC36.04.
GeneIDi2540946.
KEGGispo:SPBC36.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19052.1.
PIRiT40299.
RefSeqiNP_595332.1. NM_001021240.2.

3D structure databases

ProteinModelPortaliO59701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277462. 50 interactions.
MINTiMINT-4675483.

Proteomic databases

MaxQBiO59701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC36.04.1; SPBC36.04.1:pep; SPBC36.04.
GeneIDi2540946.
KEGGispo:SPBC36.04.

Organism-specific databases

EuPathDBiFungiDB:SPBC36.04.
PomBaseiSPBC36.04. cys11.

Phylogenomic databases

HOGENOMiHOG000217393.
InParanoidiO59701.
KOiK01738.
OMAiEDTHAEM.
OrthoDBiEOG77DJGD.
PhylomeDBiO59701.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BioCyciRETL1328306-WGS:GSTH-1819-MONOMER.
ReactomeiR-SPO-1614603. Cysteine formation from homocysteine.

Miscellaneous databases

PROiO59701.

Family and domain databases

InterProiIPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Characterization of two genes encoding putative cysteine synthase required for cysteine biosynthesis in Schizosaccharomyces pombe."
    Fujita Y., Takegawa K.
    Biosci. Biotechnol. Biochem. 68:306-311(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
    Strain: ATCC 38399.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "Multiple fungal enzymes possess cysteine synthase activity in vitro."
    Brzywczy J., Natorff R., Sienko M., Paszewski A.
    Res. Microbiol. 158:428-436(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCYSK_SCHPO
AccessioniPrimary (citable) accession number: O59701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.