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Reviewed, UniProtKB/Swiss-Prot Q6CDM0 (KYNU_YARLI)

Last modified November 3, 2009. Version 35. 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

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Names and origin

Protein namesRecommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5
Gene names
Name: BNA5
Ordered Locus Names: YALI0B22902g
OrganismYarrowia lipolytica (Candida lipolytica) [Complete proteome]
Taxonomic identifier4952 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

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Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the kynureninase family.

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Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Kynureninase
PRO_0000218664

Regions

Region127 – 1304Pyridoxal phosphate binding By similarity

Sites

Binding site991Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1001Pyridoxal 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

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Sequences

Sequence LengthMass (Da)Tools
Q6CDM0-1 [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

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Cross-references

Sequence databases

CR382128 Genomic DNA. Translation: CAG83495.1.
RefSeqXP_501242.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6CDM0.

Genome annotation databases

GeneID2906903.
GenomeReviewsGene locus YALI0B22902g in contig CR382128_GR.
KEGGyli:YALI0B22902g.

Phylogenomic databases

HOGENOMQ6CDM0.
OMAWQPLSGW.

Enzyme and pathway databases

BRENDA3.7.1.3. 3602.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

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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: November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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