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Protein

Kynurenine formamidase

Gene

kynB

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.UniRule annotation1 Publication

Catalytic activityi

N-formyl-L-kynurenine + H2O = formate + L-kynurenine.UniRule annotation1 Publication

Pathwayi: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 2 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Tryptophan 2,3-dioxygenase (kynA)
  2. Kynurenine formamidase (kynB)
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

GO - Molecular functioni

  • arylformamidase activity Source: UniProtKB
  • formamidase activity Source: InterPro

GO - Biological processi

  • anthranilate metabolic process Source: UniProtKB
  • tryptophan catabolic process to kynurenine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tryptophan catabolism

Enzyme and pathway databases

BioCyciBCER226900:GJEU-2757-MONOMER.
UniPathwayiUPA00333; UER00454.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine formamidaseUniRule annotation (EC:3.5.1.9UniRule annotation)
Short name:
KFAUniRule annotation
Short name:
KFaseUniRule annotation
Alternative name(s):
ArylformamidaseUniRule annotation
N-formylkynurenine formamidaseUniRule annotation
Short name:
FKFUniRule annotation
Gene namesi
Name:kynBUniRule annotation
Ordered Locus Names:BC_2758
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Kynurenine formamidasePRO_0000362091Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi226900.BC2758.

Structurei

3D structure databases

ProteinModelPortaliQ81CK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the KynB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107VWA. Bacteria.
COG1878. LUCA.
KOiK07130.
OMAiMDAHHRI.
OrthoDBiEOG67T5JJ.

Family and domain databases

HAMAPiMF_01969. KynB.
InterProiIPR007325. KFase.
IPR017484. Kynurenine_formamidase_bac.
[Graphical view]
PfamiPF04199. Cyclase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03035. trp_arylform. 1 hit.

Sequencei

Sequence statusi: Complete.

Q81CK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTSEWIDIS QPLNNNIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH
60 70 80 90 100
TGTHIDAPFH FDNDGKKVLD LDVQVYVGPA RIIDVSNLES IGKKELESFH
110 120 130 140 150
LEGVERLLLR TSSHGKAEEF PEVIPHLRAD IASFLSEKGI RLIGVDVPSV
160 170 180 190 200
DPLDDKELAA HHQLFKHGIH ILENVVLDHV ADGDYELIAL PLALTDADGS

PVRAVIRPI
Length:209
Mass (Da):23,066
Last modified:June 1, 2003 - v1
Checksum:i54270A35415116A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP09711.1.
RefSeqiNP_832510.1. NC_004722.1.
WP_000858074.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP09711; AAP09711; BC_2758.
GeneIDi1205106.
KEGGibce:BC2758.
PATRICi32601417. VBIBacCer54481_2813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP09711.1.
RefSeqiNP_832510.1. NC_004722.1.
WP_000858074.1. NC_004722.1.

3D structure databases

ProteinModelPortaliQ81CK1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC2758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP09711; AAP09711; BC_2758.
GeneIDi1205106.
KEGGibce:BC2758.
PATRICi32601417. VBIBacCer54481_2813.

Phylogenomic databases

eggNOGiENOG4107VWA. Bacteria.
COG1878. LUCA.
KOiK07130.
OMAiMDAHHRI.
OrthoDBiEOG67T5JJ.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00454.
BioCyciBCER226900:GJEU-2757-MONOMER.

Family and domain databases

HAMAPiMF_01969. KynB.
InterProiIPR007325. KFase.
IPR017484. Kynurenine_formamidase_bac.
[Graphical view]
PfamiPF04199. Cyclase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03035. trp_arylform. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711.
  2. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiKYNB_BACCR
AccessioniPrimary (citable) accession number: Q81CK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 1, 2003
Last modified: November 11, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.