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Reviewed, UniProtKB/Swiss-Prot Q1DZA6 (KYNU_COCIM)

Last modified February 9, 2010. Version 21. 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

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
ORF Names: CIMG_04357
OrganismCoccidioides immitis (Valley fever fungus) [Complete proteome]
Taxonomic identifier5501 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length480 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.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Kynureninase
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
Q1DZA6-1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: BDB23F5C91D5D94E

FASTA48053,525
        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        480 
DSVFSHLVDN GVILDERKPD VIRVAPAPLY NTFTDVWDFV QIFFDACRKA AQEKDTTSHG 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476727 Genomic DNA. Translation: EAS33333.1.
RefSeqXP_001244916.1.

3D structure databases

SMRQ1DZA6. Positions 18-466.
ModBaseSearch...

Genome annotation databases

GeneID4564403.

Phylogenomic databases

OrthoDBEOG9RZ0G9.
PhylomeDBQ1DZA6.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
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...

Entry information

Entry nameKYNU_COCIM
AccessionPrimary (citable) accession number: Q1DZA6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 11, 2006
Last modified: February 9, 2010
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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