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Q6CDM0 (KYNU_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kynureninase
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene names
Name:BNA5
Ordered Locus Names:YALI0B22902g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia ›

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Kynureninase HAMAP-Rule MF_03017
PRO_0000218664

Regions

Region127 – 1304Pyridoxal phosphate binding By similarity

Sites

Binding site991Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1001Pyridoxal phosphate By similarity
Binding site1831Pyridoxal phosphate By similarity
Binding site2121Pyridoxal phosphate By similarity
Binding site2151Pyridoxal phosphate By similarity
Binding site2371Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate By similarity
Binding site2951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2381N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CDM0 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 903018CA6020F2CA

FASTA43748,411
        10         20         30         40         50         60 
MPLNFRDRFN VPVLKNGEEV AYLVGNSLGL MPHKTRDYVN QEMDAWSQLG VKGHFVSGKE 

        70         80         90        100        110        120 
DLGQDVHQGP WYSCDEPLHG LVGPILGASE DEVAIMNTLT SNIHSLFSAF YKPTAKRSKI 

       130        140        150        160        170        180 
LFEAKAFPSD TYAMEAQARL HNLDPSEALI KLAPKDGLHT LSDDDIIKVI EEQGDEIAVV 

       190        200        210        220        230        240 
FFSGIQFYTG QLFDIPRITA AAKAKGCVVG WDLAHAAGNV PLKLHDWNVD FAVFCTYKYM 

       250        260        270        280        290        300 
NSGPGGIGGL FVHDKYADDQ RPRLAGWWGN NAETRFKMLD EFDPIRGARG YKQSNPSVLC 

       310        320        330        340        350        360 
VLALRASLEL FKEAGGIEKL RERSIELTNR LLKGLLASPH YIAPENIEIF GNSGKAWFTI 

       370        380        390        400        410        420 
ITPQAEHQRG AQLSLLFGPD GTMKKVFDYL DDHGVLGDER NPDVIRLAPA PLYNNERDVD 

       430 
LAIKLINDSI NLINGSA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR382128 Genomic DNA. Translation: CAG83495.1.
RefSeqXP_501242.1. XM_501242.1.

3D structure databases

ProteinModelPortalQ6CDM0.
ModBaseSearch...

Protein-protein interaction databases

STRING4952.Q6CDM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2906903.
KEGGyli:YALI0B22902g.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAMLTHVNY.
OrthoDBEOG4TB7KQ.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_YARLI
AccessionPrimary (citable) accession number: Q6CDM0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: August 16, 2004
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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