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Reviewed, UniProtKB/Swiss-Prot P0A1E3 (CYSK_SALTY)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 A
      Short name=CSase A
    EC=2.5.1.47
Alternative name(s):
    O-acetylserine sulfhydrylase A
    O-acetylserine (thiol)-lyase A
      Short name=OAS-TL A
Gene names
Name: cysK
Ordered Locus Names: STM2430
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homodimer. Ref.3

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 323322Cysteine synthase A
PRO_0000167089

Regions

Region177 – 1815Pyridoxal phosphate binding

Sites

Binding site81Allosteric inhibitor
Binding site721Pyridoxal phosphate
Binding site2691Allosteric inhibitor; via amide nitrogen
Binding site2731Pyridoxal phosphate

Amino acid modifications

Modified residue421N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict701S → N in AAA27051. Ref.1
Sequence conflict267 – 2682GI → VF in AAA27051. Ref.1

Secondary structure

.............................................................. 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A1E3-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CE74168FAAE99B9E

FASTA32334,536
        10         20         30         40         50         60 
MSKIYEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK 

        70         80         90        100        110        120 
PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM 

       130        140        150        160        170        180 
KGAIQKAEEI VASDPQKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFISGVGTGG 

       190        200        210        220        230        240 
TLTGVTRYIK GTKGKTDLIT VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPGNLD 

       250        260        270        280        290        300 
LKLIDKVVGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP 

       310        320 
SSGERYLSTA LFADLFTEKE LQQ 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH."
Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.
J. Bacteriol. 170:3150-3157(1988) [PubMed: 3290198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16 AND 321-323.
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium."
Burkhard P., Rao G.S.J., Hohenester E., Schnackerz K.D., Cook P.F., Jansonius J.N.
J. Mol. Biol. 283:121-133(1998) [PubMed: 9761678] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, SEQUENCE REVISION TO 267-268.
[4]"Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium."
Burkhard P., Tai C.-H., Ristroph C.M., Cook P.F., Jansonius J.N.
J. Mol. Biol. 291:941-953(1999) [PubMed: 10452898] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) MUTANT ALA-42 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
[5]"Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound."
Burkhard P., Tai C.-H., Jansonius J.N., Cook P.F.
J. Mol. Biol. 303:279-286(2000) [PubMed: 11023792] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, ALLOSTERIC REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21450 Genomic DNA. Translation: AAA27051.1.
AE006468 Genomic DNA. Translation: AAL21324.1.
PIRSYEBAC. B28181.
RefSeqNP_461365.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D6SX-ray2.30A/B2-323[»]
1FCJX-ray2.00A/B/C/D2-323[»]
1OASX-ray2.20A/B2-323[»]
ModBaseSearch...

Proteomic databases

PRIDEP0A1E3.

Genome annotation databases

GeneID1253952.
GenomeReviewsGene locus STM2430 in contig AE006468_GR.
KEGGstm:STM2430.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG748215.
OMAKYFMPGQ.

Enzyme and pathway databases

BioCycSTYP99287:STM2430-MONOMER.
BRENDA2.5.1.47. 2.

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_SALTY
AccessionPrimary (citable) accession number: P0A1E3
Secondary accession number(s): P12674
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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