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P0A534 (CYSK_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
O-acetylserine sulfhydrylase
Short name=OAS sulfhydrylase
Short name=OASS
EC=2.5.1.47
Alternative name(s):
Cysteine synthase A
Short name=CSase A
O-acetylserine (thiol)-lyase A
Short name=OAS-TL A
O-acetylserine-specific cysteine synthase
Sulfide-dependent cysteine synthase
Gene names
Name:cysK1
Synonyms:cysK
Ordered Locus Names:Rv2334, MT2397
ORF Names:MTCY98.03
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Ref.3

Catalytic activity

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

Cofactor

Pyridoxal phosphate. Ref.3

Enzyme regulation

Competitively inhibited by a four-residue peptide derived from the C-terminus of serine acetyltransferase (CysE). This suggests that CysK1 may associate with CysE in vivo to form a bi-enzyme complex, in which the OASS activity is down-regulated. Ref.3

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

Chain1 – 310310O-acetylserine sulfhydrylase
PRO_0000167094

Regions

Region178 – 1825Pyridoxal phosphate binding

Sites

Binding site741Pyridoxal phosphate
Binding site2661Pyridoxal phosphate

Amino acid modifications

Modified residue441N6-(pyridoxal phosphate)lysine

Secondary structure

1 ......................................................... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A534 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 597B1106CA6D0B9A

FASTA31032,753
        10         20         30         40         50         60 
MSIAEDITQL IGRTPLVRLR RVTDGAVADI VAKLEFFNPA NSVKDRIGVA MLQAAEQAGL 

        70         80         90        100        110        120 
IKPDTIILEP TSGNTGIALA MVCAARGYRC VLTMPETMSL ERRMLLRAYG AELILTPGAD 

       130        140        150        160        170        180 
GMSGAIAKAE ELAKTDQRYF VPQQFENPAN PAIHRVTTAE EVWRDTDGKV DIVVAGVGTG 

       190        200        210        220        230        240 
GTITGVAQVI KERKPSARFV AVEPAASPVL SGGQKGPHPI QGIGAGFVPP VLDQDLVDEI 

       250        260        270        280        290        300 
ITVGNEDALN VARRLAREEG LLVGISSGAA TVAALQVARR PENAGKLIVV VLPDFGERYL 

       310 
STPLFADVAD

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex."
Schnell R., Oehlmann W., Singh M., Schneider G.
J. Biol. Chem. 282:23473-23481(2007) [PubMed: 17567578] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH THE REACTION INTERMEDIATE ALPHA-AMINOACRYLATE OR PEPTIDE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, REACTION MECHANISM.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842579 Genomic DNA. Translation: CAE55474.1.
AE000516 Genomic DNA. Translation: AAK46689.1.
PIRG70660.
RefSeqNP_336875.1. NC_002755.2.
YP_177868.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3BX-ray1.80A1-310[»]
2Q3CX-ray2.10A1-310[»]
2Q3DX-ray2.20A1-310[»]
ProteinModelPortalP0A534.
SMRP0A534. Positions 1-306.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001064; EBMYCP00000001064; EBMYCG00000001064.
EBMYCT00000072085; EBMYCP00000070144; EBMYCG00000072080.
GeneID886016.
924015.
GenomeReviewsGene locus MT2397 in contig AE000516_GR.
Gene locus Rv2334 in contig AL123456_GR.
KEGGmtc:MT2397.
mtu:Rv2334.
PATRIC18127022. VBIMycTub22151_2620.
TIGRMT2397.

Organism-specific databases

TubercuListRv2334.

Phylogenomic databases

GeneTreeEBGT00050000015764.
HOGENOMHBG748215.
OMAVVIVPSF.
PhylomeDBP0A534.
ProtClustDBCLSK799368.

Enzyme and pathway databases

ReactomeREACT_27295. Mycobacterium tuberculosis biological processes.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005859. CysK.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]
KOK01738.
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR01139. CysK. 1 hit.
TIGR01136. CysKM. 1 hit.
PROSITEPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSK_MYCTU
AccessionPrimary (citable) accession number: P0A534
Secondary accession number(s): P95230
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents