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Protein

Kynureninase

Gene

kynU

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: Annotation score: 4 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-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway:iL-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (kynU)
This subpathway is part of the pathway L-kynurenine degradation, 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-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway:iNAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Kynureninase (kynU)
  3. no protein annotated in this organism
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei105 – 1051Pyridoxal phosphateUniRule annotation
Binding sitei213 – 2131Pyridoxal phosphateUniRule annotation
Binding sitei216 – 2161Pyridoxal phosphateUniRule annotation
Binding sitei238 – 2381Pyridoxal phosphateUniRule annotation
Binding sitei267 – 2671Pyridoxal phosphateUniRule annotation
Binding sitei295 – 2951Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBCER226900:GJEU-2758-MONOMER.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

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:BC_2759
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428KynureninasePRO_0000356990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ81CK0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi226900.BC2759.

Structurei

3D structure databases

ProteinModelPortaliQ81CK0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1354Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG6N67XP.

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.

Q81CK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA
60 70 80 90 100
EKSLLTLLDS WKEYGIDGWT EGEHPWFFLS EKLGKLTAPL IGALPEETIV
110 120 130 140 150
TGSTTTNIHQ VIATFYEPKG IRTKILADEL TFPSDIYALQ SQIRLKGLDP
160 170 180 190 200
EEHLVRVKSR DGRTLSEEDI IHAMEDDIAL ILLPSVLYRS GQILDMKRLT
210 220 230 240 250
TEAHKRGIHI GFDLCHSIGS IPHHFKDWDV DFAVWCNYKY LNAGPGSVAG
260 270 280 290 300
LYVNSKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS
310 320 330 340 350
TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIGHELKD FEFTIGNPLE
360 370 380 390 400
DEKRGGHIYL EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE
410 420
VWKSVQILKK IMKNEEYKQF ENKREVVA
Length:428
Mass (Da):48,754
Last modified:June 1, 2003 - v1
Checksum:i39B9A789AE41714F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP09712.1.
RefSeqiNP_832511.1. NC_004722.1.
WP_000276298.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP09712; AAP09712; BC_2759.
GeneIDi1205107.
KEGGibce:BC2759.
PATRICi32601419. VBIBacCer54481_2814.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP09712.1.
RefSeqiNP_832511.1. NC_004722.1.
WP_000276298.1. NC_004722.1.

3D structure databases

ProteinModelPortaliQ81CK0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC2759.

Proteomic databases

PRIDEiQ81CK0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP09712; AAP09712; BC_2759.
GeneIDi1205107.
KEGGibce:BC2759.
PATRICi32601419. VBIBacCer54481_2814.

Phylogenomic databases

eggNOGiCOG3844.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG6N67XP.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciBCER226900:GJEU-2758-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711.

Entry informationi

Entry nameiKYNU_BACCR
AccessioniPrimary (citable) accession number: Q81CK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 79 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

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.