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Reviewed, UniProtKB/Swiss-Prot P0C8P4 (KYNB_RALME)

Last modified May 26, 2009. Version 5. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Kynurenine formamidase
      Short name=KFA
    EC=3.5.1.9
Alternative name(s):
    N-formylkynurenine formamidase
Gene names
Name: kynB
Ordered Locus Names: Rmet_2648
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine. Ref.2 Ref.3

Catalytic activity

N-formyl-L-kynurenine + H2O = formate + L-kynurenine. Ref.2 Ref.3

Enzyme regulation

Inhibited by EDTA. Insensitive to PMSF. Ref.2 Ref.3

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2. Ref.3

Sequence similarities

Belongs to the kynB family.

Biophysicochemical properties

Kinetic parameters:

KM=75 µM for N-formyl-L-kynurenine

pH dependence:

Optimum pH is 8.0.

Sequence caution

The sequence CP000352 differs from that shown. Reason: Erroneous termination at position 83. Translated as Tyr.

Ontologies

Keywords
   Biological processTryptophan catabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processanthranilate metabolic process Ref.3

Inferred from direct assay. Source: UniProtKB

tryptophan catabolic process to kynurenine Ref.3

Inferred from direct assay. Source: UniProtKB

   Molecular functionarylformamidase activity Ref.3

Inferred from direct assay. Source: UniProtKB

metal ion binding Ref.3

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Kynurenine formamidase
PRO_0000362135

Sequences

Sequence LengthMass (Da)Tools
P0C8P4-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 43F8AEFAEA1959D9

FASTA21823,383
        10         20         30         40         50         60 
MPQAPQLHDG RRIWDISPAV SPATPVWPGD TPFQHDPAWQ LDEHCPVNVG RITMSPHTGA 

        70         80         90        100        110        120 
HADAPLHYAA DGAPIGAVPL DAYLGPCRVI HCIGAAPRVE PQHIAHALAG TPPRVLLRTY 

       130        140        150        160        170        180 
AQAPQGKWDS AFCAVAPETI SLLARHGVRL IGIDTPSLDP ETSKTMDAHH AVRDHQLAIL 

       190        200        210 
EGIVLDEVPA GDYELIALPL RLATLDASPV RAVLRELP 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria."
Kurnasov O., Goral V., Colabroy K., Gerdes S., Anantha S., Osterman A., Begley T.P.
Chem. Biol. 10:1195-1204(2003) [PubMed: 14700627] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase."
Kurnasov O., Jablonski L., Polanuyer B., Dorrestein P., Begley T., Osterman A.
FEMS Microbiol. Lett. 227:219-227(2003) [PubMed: 14592712] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, PATHWAY.

Cross-references

Sequence databases

CP000352 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus Rmet_2648 in contig CP000352_GR.
KEGGrme:Rmet_2648.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR017484. Arylformamidase.
IPR007325. Cyclase.
[Graphical view]
PfamPF04199. Cyclase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03035. trp_arylform. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNB_RALME
AccessionPrimary (citable) accession number: P0C8P4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: May 26, 2009
This is version 5 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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