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Reviewed, UniProtKB/Swiss-Prot P60068 (CLRA_IDEDE)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chlorate reductase subunit alpha
    EC=1.97.1.1
Alternative name(s):
    Chlorate reductase molybdenum subunit
Gene names
Name: clrA
OrganismIdeonella dechloratans
Taxonomic identifier36863 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesIdeonella

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Terminal reductase that allows anaerobic growth on chlorate as the sole respiratory oxidant.

Catalytic activity

AH2 + chlorate = A + H2O + chlorite.

Cofactor

Binds 1 4Fe-4S cluster Potential.

Molybdenum (molybdopterin).

Subunit structure

Heterotrimer of alpha, beta and gamma subunits.

Subcellular location

Periplasm.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Biotechnological use

Has potential use in bioremediation of waste sites contaminated with chlorate, such as pulp and paper industry wastewater.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
Molybdenum
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

chlorate reductase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

molybdenum ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232Tat-type signal Potential
Chain33 – 914882Chlorate reductase subunit alpha
PRO_0000019173

Sites

Metal binding691Iron-sulfur (4Fe-4S); via pros nitrogen By similarity
Metal binding731Iron-sulfur (4Fe-4S) By similarity
Metal binding771Iron-sulfur (4Fe-4S) By similarity
Metal binding1111Iron-sulfur (4Fe-4S) By similarity
Metal binding2051Molybdenum By similarity

Sequences

Sequence LengthMass (Da)Tools
P60068-1 [UniParc].

Last modified November 28, 2003. Version 1.
Checksum: 372B1FDE26E06499

FASTA914102,823
        10         20         30         40         50         60 
MNSPDEHNGR RRFLQFSAAA LASAAASPSL WAFSKIQPIE DPLKDYPYRD WEDLYRKEWT 

        70         80         90        100        110        120 
WDSVGVMTHS NGCVAGCAWN VFVKNGIPMR EEQISKYPQL PGIPDMNPRG CQKGAVYCSW 

       130        140        150        160        170        180 
SKQPDHIKWP LKRVGERGER KWKRISWDEA LTEIADKIID TTVKRGPGNI YIPKRPFAVI 

       190        200        210        220        230        240 
TNTAYTRMTK LLGAISPDAT SMTGDLYTGI QTVRVPASTV STFDDWFTSD LILMWHKNPI 

       250        260        270        280        290        300 
VTRIPDAHFL MEARYNGARL VNISADYNPS SIHSDLFVPV TSGTDSHLAA ALVNVLIAGK 

       310        320        330        340        350        360 
HYKADYLKEQ TALPFLVRTD NGKFLREKDF KADGSDQVFY VWDTKAGKAV LAPGSMGSKD 

       370        380        390        400        410        420 
KTLKLGTIDP ALEGNFETHG IKVTTVFERL KAEITPYTPE ATQATTGVHP SVVRQLAGWI 

       430        440        450        460        470        480 
AECKALRILD GYNNQKHFDG FQCGRLKILI LTLIGHHGTT GSIDTTFEGW RLEGNSELGT 

       490        500        510        520        530        540 
VKGKPGRSVS AVLAQWVWGE QYQRSKDYFN DAQLREELGF GVDEMESMRK ESEANGWMPN 

       550        560        570        580        590        600 
WQSIKEPVVS ITGGINMFAT SNGYQHLRDN FLKRCELNVV VDFRLNSGAM YADIVLPAAE 

       610        620        630        640        650        660 
NTEKLDIRET SVTRFIHAFG QPVKPMYERK TDWQIMVALA AKIQERAKAR GIARVDDPEI 

       670        680        690        700        710        720 
KSGIDFDKIY DEFTMNGKVV TDEQAVRFVM DNSKALGPGT YEEVMKNGFV AVGPSAGKTG 

       730        740        750        760        770        780 
PVPKDKPYRP FTVNVTDKKP YGTLTGRLQF YVDHDWFQRL GATVPKPQYR GGVLGPKKYP 

       790        800        810        820        830        840 
FVRNSPHARW GVHSFARTEQ WMLRHQRGEP DVRMSPKAMA AKGIKDGDMV RIFNDSGEFF 

       850        860        870        880        890        900 
AVVKAMPALP DNMLFTEHGW EQYQYKNMTH YNMVSSELIN PLELVGGYGH IKYTSGGFNP 

       910 
NRIFYETTVD VEKA 

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References

[1]"A gene cluster for chlorate metabolism in Ideonella dechloratans."
Danielsson Thorell H., Stenklo K., Karlsson J., Nilsson T.
Appl. Environ. Microbiol. 69:5585-5592(2003) [PubMed: 12957948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Cross-references

Sequence databases

AJ566363 Genomic DNA. Translation: CAD97447.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB5.A.3.8.2. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Enzyme and pathway databases

BRENDA1.97.1.1. 189170.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_fold.
IPR017840. DMSO_Rdtase_II_Mopterin_su.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006657. MPT_dinuc_bd.
IPR006311. Tat.
IPR017909. Twin_arg_translocation_Tat.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
PfamPF00384. Molybdopterin. 2 hits.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR03479. DMSO_red_II_alp. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. False negative.
PS00490. MOLYBDOPTERIN_PROK_2. False negative.
PS00932. MOLYBDOPTERIN_PROK_3. False negative.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLRA_IDEDE
AccessionPrimary (citable) accession number: P60068
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents