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Reviewed, UniProtKB/Swiss-Prot P80608 (CYSK_MAIZE)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cysteine synthase
      Short name=CSase
    EC=2.5.1.47
Alternative name(s):
    O-acetylserine sulfhydrylase
    O-acetylserine (thiol)-lyase
      Short name=OAS-TL
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACCAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

O(3)-acetyl-L-serine + H2S = L-cysteine + acetate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cysteine synthase/cystathionine beta-synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcysteine biosynthetic process from serine

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine synthase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Cysteine synthase
PRO_0000167120

Regions

Region184 – 1885Pyridoxal phosphate binding By similarity
Compositional bias275 – 2806Poly-Ala

Sites

Binding site801Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue491N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P80608-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3213A69326D7CEED

FASTA32534,207
        10         20         30         40         50         60 
MGEASPSIAK DVTELIGNTP LVYLNKVTDG CVGRSRAKLE SMEPCSSVKD RIGYSMITDA 

        70         80         90        100        110        120 
EEKGLITPGV SVLIEPTSGN TGIGLAFMAA AKGYKLTLTM PASMSMERRI ILKAFGAELV 

       130        140        150        160        170        180 
LTDPLLGMKG AVKKAEEIQA KTPNSYILQQ FENPANPKIH YETTGPEIWK ATAGKIDGLV 

       190        200        210        220        230        240 
SGIGTGGTIT GTGRYLREQN PNVKLYGVEP VESAVLNGGK PGPHKIQGIG AGFIPGVLDV 

       250        260        270        280        290        300 
DLLDETLQVS SDEAIETAKA LALKEGLLVG ISSGAAAAAA VRLAKRPENA GKLFVVVFPS 

       310        320 
FGERYLSSVL FQSIKKEAES MVVEP 

« Hide

References

[1]"Isolation of a cDNA encoding a putative chloroplastic isoform of cysteine synthase from maize."
Brander K.A., Owttrim G.W., Brunold C.
Plant Gene Register PGR95-031
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. B73.
Tissue: Root.
[2]"The maize two dimensional gel protein database: towards an integrated genome analysis program."
Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C., Zivy M., de Vienne D.
Theor. Appl. Genet. 93:997-1005(1996) [Agricola: IND20551642]
Cited for: PROTEIN SEQUENCE OF 11-25.
Tissue: Coleoptile.

Cross-references

Sequence databases

X85803 mRNA. Translation: CAA59798.1.
PIRS52738.
RefSeqNP_001105469.1.
UniGeneZm.93961

3D structure databases

HSSPHSSP built from PDB template 1FCJ based on UniProtKB P12674.
SMRP80608. Positions 8-324.
ModBaseSearch...

Genome annotation databases

GeneID542438.

Organism-specific databases

GrameneP80608.
MaizeGDB123922.

Enzyme and pathway databases

BRENDA2.5.1.47. 289.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005859. CysK.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
TIGRFAMsTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSK_MAIZE
AccessionPrimary (citable) accession number: P80608
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents