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Reviewed, UniProtKB/Swiss-Prot Q750P5 (KYNU_ASHGO)

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: AGL098W
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

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Protein attributes

Sequence length447 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 – 447447Kynureninase
PRO_0000218661

Regions

Region134 – 1374Pyridoxal phosphate binding By similarity

Sites

Binding site1061Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1071Pyridoxal phosphate By similarity
Binding site2201Pyridoxal phosphate By similarity
Binding site2231Pyridoxal phosphate By similarity
Binding site2451Pyridoxal phosphate By similarity
Binding site2751Pyridoxal phosphate By similarity
Binding site3031Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2461N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q750P5-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6C0AA0A05795D63A

FASTA44749,069
        10         20         30         40         50         60 
MEKARALEEQ WPGARDAFHV PSYASLGLGD QTAAVRYLCG HSLGCMPRKT RGSVEAELSA 

        70         80         90        100        110        120 
WSARAVEAHV RHPGGTEWVN TDLPLVPQMA RMVGASQQEV AVMGSLTANL NALLVAFYRP 

       130        140        150        160        170        180 
RGRRTKILLE KQVFPSDFHA FWNQAALHGL DPAATLVQVA PRAGEHTLRT EDIVPAIETH 

       190        200        210        220        230        240 
RAELALVCLP GVQYYTGQLL DMASIVAAAR REPSIVVGFD LAHAVGNVQL QLHEWGADFA 

       250        260        270        280        290        300 
CWCSYKYLNA GPGGIAGLFV HEHHHGGTLP RLTGWWGTNA ATRFEMRQTY DPLPDALGFR 

       310        320        330        340        350        360 
QSNPSVLDVA ALRASLEVFE DFGGMERVRA RSLALTGYLY ELLTQSVFYR PEVGADGVGF 

       370        380        390        400        410        420 
TILTPANPAE RGAQLSLLFW PHSDDPDKNT MPRVFADLRQ NGVLGDERHP DVIRLTPCAL 

       430        440 
YNTFMEVFES VQLLNAALER LAPESAV

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References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

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Cross-references

Sequence databases

AE016820 Genomic DNA. Translation: AAS54393.1.
RefSeqNP_986569.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ750P5.

Genome annotation databases

GeneID4622868.
GenomeReviewsGene locus AGL098W in contig AE016820_GR.
KEGGago:AGOS_AGL098W.
NMPDRfig|33169.1.peg.4214.

Organism-specific databases

AGDAGL098W.

Phylogenomic databases

HOGENOMQ750P5.
OMANFPTDVY.

Enzyme and pathway databases

BRENDA3.7.1.3. 279361.

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_ASHGO
AccessionPrimary (citable) accession number: Q750P5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: July 5, 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