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Q1DZA6 (KYNU_COCIM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 43. 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
ORF Names:CIMG_04357
OrganismCoccidioides immitis (strain RS) (Valley fever fungus) [Reference proteome]
Taxonomic identifier246410 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides ›

Protein attributes

Sequence length478 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 – 478478Kynureninase HAMAP-Rule MF_03017
PRO_0000360868

Regions

Region166 – 1694Pyridoxal phosphate binding By similarity

Sites

Binding site1381Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1391Pyridoxal phosphate By similarity
Binding site2521Pyridoxal phosphate By similarity
Binding site2551Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate By similarity
Binding site3151Pyridoxal phosphate By similarity
Binding site3431Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1DZA6 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: 6F5C91D5D94E8873

FASTA47853,331
        10         20         30         40         50         60 
MVDSSKAPLP FRDSALSFKR EYAESLDAQD PLREFRNQFI IPSKADLKRK SLAVAEGESP 

        70         80         90        100        110        120 
SSDCIYLCGN SLGLQPKNAR MYIDRFLQTW ATKAVLGHFT KLEDSPFPPY MDYDDVTSKL 

       130        140        150        160        170        180 
MAQVVGALPS EVAVMSTLTG NLHLLMASFY RPTKEKYKII LEGKAFPSDH YAVESQIRHH 

       190        200        210        220        230        240 
GFDPKDAMVL IEPKDLKEPV LPTERILKTI DEHASSTALI LLPGIQYYSG QYLDIPTITA 

       250        260        270        280        290        300 
HAHSKGLLIG WDCAHAAGNV ELKLHDWDVD FAAWCTYKYV NSGPGSMGAL FVHEKHGQVN 

       310        320        330        340        350        360 
LENKEDPYRH RLTGWWGGDK SLRFLMDNNF VPRPGAAGFQ LSNPSVLDMT AVLSSLDIFD 

       370        380        390        400        410        420 
KATMPALRKK SLELTAYLEH LLLNSPEGVR PSDDPFSIIT PSDPEARGAQ LSVLLKPGLL 

       430        440        450        460        470 
DSVFSHLVDN GVILDERKPD VIRVAPAPLY NTFTDVWDFV QIFFDACRKA AQEKDTTS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		GG704914 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalQ1DZA6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_COCIM
AccessionPrimary (citable) accession number: Q1DZA6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 9, 2013
Last modified: May 1, 2013
This is version 43 of the entry and version 2 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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