Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

L-cysteine/cystine lyase C-DES

Gene

c-des

Organism
Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714))
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

pyridoxal 5'-phosphateUniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei114 – 1141Important for catalytic activityCombined sources
Sitei197 – 1971Important for catalytic activityCombined sources
Binding sitei223 – 2231N6-(pyridoxalphosphate)lysine 1 (covalent)Combined sources
Sitei223 – 2231Important for catalytic activityCombined sources
Binding sitei251 – 2511N6-(pyridoxalphosphate)lysine 2Combined sources
Binding sitei276 – 2761N6-(pyridoxalphosphate)lysine 2Combined sources

GO - Molecular functioni

  1. lyase activity Source: UniProtKB-KW
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

Pyridoxal phosphateSAAS annotation

Enzyme and pathway databases

SABIO-RKQ9ZHG9.

Names & Taxonomyi

Protein namesi
Submitted name:
L-cysteine/cystine lyase C-DESImported
Gene namesi
Name:c-desImported
OrganismiSynechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714))Imported
Taxonomic identifieri1147 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELQX-ray1.80A/B4-393[»]
1ELUX-ray1.55A/B4-393[»]
1N2TX-ray2.00A/B9-393[»]
1N31X-ray2.20A/B9-393[»]
ProteinModelPortaliQ9ZHG9.
SMRiQ9ZHG9. Positions 13-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZHG9.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZHG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPVNLIPD RHQFPGLANK TYFNFGGQGI LPTVALEAIT AMYGYLQENG
60 70 80 90 100
PFSIAANQHI QQLIAQLRQA LAETFNVDPN TITITDNVTT GCDIVLWGLD
110 120 130 140 150
WHQGDEILLT DCEHPGIIAI VQAIAARFGI TYRFFPVAAT LNQGDAAAVL
160 170 180 190 200
ANHLGPKTRL VILSHLLWNT GQVLPLAEIM AVCRRHQGNY PVRVLVDGAQ
210 220 230 240 250
SAGSLPLDFS RLEVDYYAFT GHKWFAGPAG VGGLYIHGDC LGEINPTYVG
260 270 280 290 300
WRSITYGAKG EPTGWAEGGK RFEVATSAYP QYAGLLAALQ LHQRQGTAEE
310 320 330 340 350
RYQAICQRSE FLWRGLNQLP HVHCLATSAP QAGLVSFTVD SPLGHRAIVQ
360 370 380 390
KLEEQRIYLR TIADPDCIRA CCHYITDEEE INHLLARLAD FGP
Length:393
Mass (Da):43,154
Last modified:May 1, 1999 - v1
Checksum:i4AC0ADA899A3264C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061964 Genomic DNA. Translation: AAD02935.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061964 Genomic DNA. Translation: AAD02935.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELQX-ray1.80A/B4-393[»]
1ELUX-ray1.55A/B4-393[»]
1N2TX-ray2.00A/B9-393[»]
1N31X-ray2.20A/B9-393[»]
ProteinModelPortaliQ9ZHG9.
SMRiQ9ZHG9. Positions 13-393.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ9ZHG9.

Miscellaneous databases

EvolutionaryTraceiQ9ZHG9.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin."
    Leibrecht I., Kessler D.
    J. Biol. Chem. 272:10442-10447(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PCC 6714Imported.
  2. "Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. Analyses using cystine analogues and recombinant C-DES."
    Lang T., Kessler D.
    J. Biol. Chem. 274:189-195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PCC 6714Imported.
  3. "Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis."
    Clausen T., Kaiser J.T., Steegborn C., Huber R., Kessler D.
    Proc. Natl. Acad. Sci. U.S.A. 97:3856-3861(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 4-393 IN COMPLEX WITH N6-(PYRIDOXALPHOSPHATE)LYSINE, ACTIVE SITE.
  4. "Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state."
    Kaiser J.T., Bruno S., Clausen T., Huber R., Schiaretti F., Mozzarelli A., Kessler D.
    J. Biol. Chem. 278:357-365(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 9-393 IN COMPLEX WITH N6-(PYRIDOXALPHOSPHATE)LYSINE, ACTIVE SITE.

Entry informationi

Entry nameiQ9ZHG9_SYNY4
AccessioniPrimary (citable) accession number: Q9ZHG9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.