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Q9ZHG9 (Q9ZHG9_SYNY4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesSubmitted name:
L-cysteine/cystine lyase C-DES EMBL AAD02935.1
Gene names
Name:c-des EMBL AAD02935.1
OrganismSynechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714)) EMBL AAD02935.1
Taxonomic identifier1147 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS020578 RuleBase RU004504

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. RuleBase RU004075

Ontologies

Keywords
   LigandPyridoxal phosphate SAAS SAAS020578
   Molecular functionLyase EMBL AAD02935.1
   Technical term3D-structure PDB 1ELQ PDB 1N31 PDB 1ELU PDB 1N2T
Gene Ontology (GO)
   Molecular_functionlyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1141Proton donor/acceptor PDB 1N2T
Binding site3601Substrate PDB 1N2T
Site1141Important for catalytic activity PDB 1ELQ
Site1971Important for catalytic activity PDB 1ELQ PDB 1N2T
Site1991Important for catalytic activity PDB 1N2T
Site2001Important for catalytic activity PDB 1N2T
Site2231Important for catalytic activity PDB 1ELQ PDB 1N2T

Amino acid modifications

Modified residue2231N6-(pyridoxal phosphate)lysine PDB 1ELQ

Sequences

Sequence LengthMass (Da)Tools
Q9ZHG9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4AC0ADA899A3264C

FASTA39343,154
        10         20         30         40         50         60 
MADPVNLIPD RHQFPGLANK TYFNFGGQGI LPTVALEAIT AMYGYLQENG PFSIAANQHI 

        70         80         90        100        110        120 
QQLIAQLRQA LAETFNVDPN TITITDNVTT GCDIVLWGLD WHQGDEILLT DCEHPGIIAI 

       130        140        150        160        170        180 
VQAIAARFGI TYRFFPVAAT LNQGDAAAVL ANHLGPKTRL VILSHLLWNT GQVLPLAEIM 

       190        200        210        220        230        240 
AVCRRHQGNY PVRVLVDGAQ SAGSLPLDFS RLEVDYYAFT GHKWFAGPAG VGGLYIHGDC 

       250        260        270        280        290        300 
LGEINPTYVG WRSITYGAKG EPTGWAEGGK RFEVATSAYP QYAGLLAALQ LHQRQGTAEE 

       310        320        330        340        350        360 
RYQAICQRSE FLWRGLNQLP HVHCLATSAP QAGLVSFTVD SPLGHRAIVQ KLEEQRIYLR 

       370        380        390 
TIADPDCIRA CCHYITDEEE INHLLARLAD FGP

« Hide

References

[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 6714 EMBL AAD02935.1.
[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 6714 EMBL AAD02935.1.
[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 12-393, ACTIVE SITE, AND PYRIDOXAL PHOSPHATE AT LYS-223.
[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, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF061964 Genomic DNA. Translation: AAD02935.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELQX-ray1.80A/B12-393[»]
1ELUX-ray1.55A/B12-393[»]
1N2TX-ray2.00A/B9-393[»]
1N31X-ray2.20A/B9-393[»]
ProteinModelPortalQ9ZHG9.
SMRQ9ZHG9. Positions 13-393.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ9ZHG9.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZHG9.

Entry information

Entry nameQ9ZHG9_SYNY4
AccessionPrimary (citable) accession number: Q9ZHG9
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info