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P16703 (CYSM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Cysteine synthase B
Short name=CSase B
EC=2.5.1.47
Alternative name(s):
O-acetylserine (thiol)-lyase B
Short name=OAS-TL B
O-acetylserine sulfhydrylase B
Gene names
Name:cysM
Ordered Locus Names:b2421, JW2414
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
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.5

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Cysteine synthase B
PRO_0000167108

Regions

Region174 – 1785Pyridoxal phosphate binding

Sites

Binding site711Pyridoxal phosphate
Binding site2551Pyridoxal phosphate

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine

Secondary structure

1 ............................................................. 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16703 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 1C7FBCB943FCFE39

FASTA30332,664
        10         20         30         40         50         60 
MSTLEQTIGN TPLVKLQRMG PDNGSEVWLK LEGNNPAGSV KDRAALSMIV EAEKRGEIKP 

        70         80         90        100        110        120 
GDVLIEATSG NTGIALAMIA ALKGYRMKLL MPDNMSQERR AAMRAYGAEL ILVTKEQGME 

       130        140        150        160        170        180 
GARDLALEMA NRGEGKLLDQ FNNPDNPYAH YTTTGPEIWQ QTGGRITHFV SSMGTTGTIT 

       190        200        210        220        230        240 
GVSRFMREQS KPVTIVGLQP EEGSSIPGIR RWPTEYLPGI FNASLVDEVL DIHQRDAENT 

       250        260        270        280        290        300 
MRELAVREGI FCGVSSGGAV AGALRVAKAN PDAVVVAIIC DRGDRYLSTG VFGEEHFSQG 


AGI

« Hide

References

« Hide 'large scale' references
[1]"Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide sequence and expression of the cysTWAM gene cluster."
Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A.
J. Bacteriol. 172:3351-3357(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli."
Claus M.T., Zocher G.E., Maier T.H.P., Schulz G.E.
Biochemistry 44:8620-8626(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT CYSM-RKE IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M32101 Genomic DNA. Translation: AAA23640.1.
U00096 Genomic DNA. Translation: AAC75474.1.
AP009048 Genomic DNA. Translation: BAA16295.1.
PIRSYECBC. D35402.
RefSeqNP_416916.1. NC_000913.2.
YP_490657.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BHSX-ray2.67A/B/C/D1-303[»]
2BHTX-ray2.10A/B/C/D1-303[»]
2V03X-ray1.33A1-303[»]
ProteinModelPortalP16703.
SMRP16703. Positions 2-293.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9383N.
IntActP16703. 9 interactions.
MINTMINT-1300981.
STRING511145.b2421.

2D gel databases

SWISS-2DPAGEP16703.

Proteomic databases

PaxDbP16703.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75474; AAC75474; b2421.
BAA16295; BAA16295; BAA16295.
GeneID12930332.
946888.
KEGGecj:Y75_p2382.
eco:b2421.
PATRIC32120227. VBIEscCol129921_2516.

Organism-specific databases

EchoBASEEB0190.
EcoGeneEG10193. cysM.

Phylogenomic databases

eggNOGCOG0031.
HOGENOMHOG000217394.
KOK12339.
OMACEVALRI.
ProtClustDBPRK11761.

Enzyme and pathway databases

BioCycEcoCyc:ACSERLYB-MONOMER.
ECOL316407:JW2414-MONOMER.
MetaCyc:ACSERLYB-MONOMER.
SABIO-RKP16703.
UniPathwayUPA00136; UER00200.

Gene expression databases

GenevestigatorP16703.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005858. CysM.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR01136. cysKM. 1 hit.
TIGR01138. cysM. 1 hit.
PROSITEPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16703.

Entry information

Entry nameCYSM_ECOLI
AccessionPrimary (citable) accession number: P16703
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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