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Q05582 (CAS2_STRCL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

EC=1.14.11.21
Alternative name(s):
Clavaminic acid synthase 2
Short name=CAS2
Short name=CS2
Gene names
Name:cs2
OrganismStreptomyces clavuligerus
Taxonomic identifier1901 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length325 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 By similarity.

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 termDirect protein sequencing
Gene Ontology (GO)
   Biological processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionclavaminate synthase activity

Inferred from electronic annotation. Source: 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 – 325324Clavaminate synthase 2
PRO_0000089323

Sites

Metal binding1451Iron By similarity
Metal binding1471Iron By similarity
Metal binding2801Iron By similarity
Binding site29412-oxoglutarate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05582 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 98C03A901B371B0E

FASTA32535,840
        10         20         30         40         50         60 
MASPIVDCTP YRDELLALAS ELPEVPRADL HGFLDEAKTL AARLPEGLAA ALDTFNAVGS 

        70         80         90        100        110        120 
EDGYLLLRGL PVDDSELPET PTSTPAPLDR KRLVMEAMRA LAGRRLGLHT GYQELRSGTV 

       130        140        150        160        170        180 
YHDVYPSPGA HYLSSETSET LLEFHTEMAY HILQPNYVML ACSRADHENR AETLVGSVRK 

       190        200        210        220        230        240 
ALPLLDEKTR ARLFDRKVPC CVDVAFRGGV DDPGAIANVK PLYGDANDPF LGYDRELLAP 

       250        260        270        280        290        300 
EDPADKEAVA HLSQALDDVT VGVKLVPGDV LIIDNFRTTH ARTPFSPRWD GKDRWLHRVY 

       310        320 
IRTDRNGELS GGERAGDTIS FSPRR 

« 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: 1472501] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24.
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: 7876185] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06214 Genomic DNA. Translation: AAA26723.1.

3D structure databases

ProteinModelPortalQ05582.
SMRQ05582. Positions 6-324.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13487.

Family and domain databases

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

Entry information

Entry nameCAS2_STRCL
AccessionPrimary (citable) accession number: Q05582
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 23, 2007
Last modified: June 28, 2011
This is version 60 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families