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Protein

Kynureninase

Gene

kynU

Organism
Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.UniRule annotation

Catalytic activityi

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • pyridoxal 5'-phosphateUniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei98 – 981Pyridoxal phosphateUniRule annotation
Binding sitei201 – 2011Pyridoxal phosphateUniRule annotation
Binding sitei204 – 2041Pyridoxal phosphateUniRule annotation
Binding sitei226 – 2261Pyridoxal phosphateUniRule annotation
Binding sitei256 – 2561Pyridoxal phosphateUniRule annotation
Binding sitei282 – 2821Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Pyridine nucleotide biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotation
Ordered Locus Names:BN118_3515Imported
OrganismiBordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323)Imported
Taxonomic identifieri568706 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000005250: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliJ7QH41.
SMRiJ7QH41. Positions 2-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1324Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

KOiK01556.
OMAiRFWQPLS.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

J7QH41-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTRQACLEA DRRDPLAAFK DEFELPAGLI YLDGNSLGAL PRGAAARAAQ
60 70 80 90 100
VIGQEWGQGL IRSWNTAGWF ELPARLGNKL AGLIGAGQDE VVMTDSTSLN
110 120 130 140 150
IFKALAAALR LAQRAAPQRK VIVSERDNFP TDLYMIQGMI DLLRQGYELR
160 170 180 190 200
LVDAGLSLEQ ALDDDVAVVL LSHVNYRTGA MHDMAAVSRR AHARGALIIW
210 220 230 240 250
DLAHAAGAVP VALDADGADF AVGCTYKYLN GGPGSPAFIW VAPRHRDDFW
260 270 280 290 300
QPLSGWWGHR QPFEMADTYV PAQGIRRYLC GTQPIVSLAT AECGLDIALR
310 320 330 340 350
ADIAQVRAKS LALGDRFIAL VESRCADHPL TLATPREHAR RGSHVSFLHP
360 370 380 390 400
QGYAVMQALI ARGVIGDYRE PELLRFGLTP LYLSHADIWD AVEILREVLD
410
TRAWDRPQYR ERAAVT
Length:416
Mass (Da):45,694
Last modified:October 31, 2012 - v1
Checksum:i7DCA08DCDD5AA37B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE965805 Genomic DNA. Translation: CCJ64940.1.
RefSeqiYP_006627955.1. NC_018518.1.

Genome annotation databases

EnsemblBacteriaiCCJ64940; CCJ64940; BN118_3515.
GeneIDi13803207.
KEGGibper:BN118_3515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE965805 Genomic DNA. Translation: CCJ64940.1.
RefSeqiYP_006627955.1. NC_018518.1.

3D structure databases

ProteinModelPortaliJ7QH41.
SMRiJ7QH41. Positions 2-404.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCJ64940; CCJ64940; BN118_3515.
GeneIDi13803207.
KEGGibper:BN118_3515.

Phylogenomic databases

KOiK01556.
OMAiRFWQPLS.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of the classical Bordetella subspecies: the evolution and exchange of virulence-associated diversity amongst closely related pathogens."
    Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.
    BMC Genomics 13:545-545(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 9797 / DSM 5571 / NCTC 10739 / 18323Imported.

Entry informationi

Entry nameiJ7QH41_BORP1
AccessioniPrimary (citable) accession number: J7QH41
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 2012
Last sequence update: October 31, 2012
Last modified: February 4, 2015
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.