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Q05581 (CAS1_STRC2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

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

Names and origin

Protein namesRecommended name:
Clavaminate synthase 1

EC=1.14.11.21
Alternative name(s):
Clavaminic acid synthase 1
Short name=CAS1
Short name=CS1
Gene names
Name:cs1
OrganismStreptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)
Taxonomic identifier443255 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2.

Proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O.

Dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O.

Cofactor

Binds 1 Fe2+ ion per subunit.

Pathway

Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 3/8.

Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 5/8.

Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 6/8.

Sequence similarities

Belongs to the clavaminate synthase family.

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

clavulanic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionclavaminate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 324323Clavaminate synthase 1
PRO_0000089322

Sites

Metal binding1441Iron
Metal binding1461Iron
Metal binding2791Iron
Binding site29312-oxoglutarate By similarity

Secondary structure

................................................................ 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05581 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F5C251134CA4933E

FASTA32435,370
        10         20         30         40         50         60 
MTSVDCTAYG PELRALAARL PRTPRADLYA FLDAAHTAAA SLPGALATAL DTFNAEGSED 

        70         80         90        100        110        120 
GHLLLRGLPV EADADLPTTP SSTPAPEDRS LLTMEAMLGL VGRRLGLHTG YRELRSGTVY 

       130        140        150        160        170        180 
HDVYPSPGAH HLSSETSETL LEFHTEMAYH RLQPNYVMLA CSRADHERTA ATLVASVRKA 

       190        200        210        220        230        240 
LPLLDERTRA RLLDRRMPCC VDVAFRGGVD DPGAIAQVKP LYGDADDPFL GYDRELLAPE 

       250        260        270        280        290        300 
DPADKEAVAA LSKALDEVTE AVYLEPGDLL IVDNFRTTHA RTPFSPRWDG KDRWLHRVYI 

       310        320 
RTDRNGQLSG GERAGDVVAF TPRG 

« Hide

References

[1]"Two isozymes of clavaminate synthase central to clavulanic acid formation: cloning and sequencing of both genes from Streptomyces clavuligerus."
Marsh E.N., Chang M.D.-T., Townsend C.A.
Biochemistry 31:12648-12657(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[2]"Expression and purification of two isozymes of clavaminate synthase and initial characterization of the iron binding site. General error analysis in polymerase chain reaction amplification."
Busby R.W., Chang M.D.-T., Busby R.C., Wimp J., Townsend C.A.
J. Biol. Chem. 270:4262-4269(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[3]"Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase."
Zhang Z., Ren J.-S., Stammers D.K., Baldwin J.E., Harlos K., Schofield C.J.
Nat. Struct. Biol. 7:127-133(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS).
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[4]"Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements."
Zhang Z., Ren J.-S., Harlos K., McKinnon C.H., Clifton I.J., Schofield C.J.
FEBS Lett. 517:7-12(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06213 Genomic DNA. Translation: AAA26722.1.
PIRA44241.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DRTX-ray2.10A1-324[»]
1DRYX-ray1.40A1-324[»]
1DS0X-ray1.63A1-324[»]
1DS1X-ray1.08A1-324[»]
1GVGX-ray1.54A1-324[»]
ProteinModelPortalQ05581.
SMRQ05581. Positions 2-324.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00112; UER00244.
UPA00112; UER00246.
UPA00112; UER00247.

Family and domain databases

InterProIPR014503. Clavaminate_syn.
IPR003819. Taurine_dOase.
[Graphical view]
PfamPF02668. TauD. 2 hits.
[Graphical view]
PIRSFPIRSF019543. Clavaminate_syn. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ05581.

Entry information

Entry nameCAS1_STRC2
AccessionPrimary (citable) accession number: Q05581
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways