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P0CO53 (KYNU_CRYNB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:CNBC3200
OrganismCryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) [Complete proteome]
Taxonomic identifier283643 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length453 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. HAMAP-Rule MF_03017

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. HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03017.

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_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: UniProtKB-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 – 453453Kynureninase HAMAP-Rule MF_03017
PRO_0000410131

Regions

Region142 – 1454Pyridoxal phosphate binding By similarity

Sites

Binding site1141Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1151Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2581N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CO53 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 36FC6C0CDDB4A102

FASTA45351,170
        10         20         30         40         50         60 
MSNDLPTKKD LVKWDQEDAL NWTRGEYEIP NSKACGGEAD GKAIYFCGNS LGLLNKKARQ 

        70         80         90        100        110        120 
HIMEELDVWS TSSVTGHFNH PYQRPWKHVD EPLTPHLAKL VGAREEEVAH TSTLTSNMHN 

       130        140        150        160        170        180 
LFTSFYQPTE KRWKIVIEKG SFPSDWYAVH SHPRLHDKVL RPEQIDNAII ALVPREGEDT 

       190        200        210        220        230        240 
LRTEDILKVL DDNKDSIAIV WLPLVQYYTG QLFDISSISP KVHEIGALLG LDMAHGIGNV 

       250        260        270        280        290        300 
ECKLNEWNVD FAVWCTYKYL NAGPAAIGGF YIRSGLEDGG RRLAGWWGND ARTRFHMSPN 

       310        320        330        340        350        360 
FQPTPGAKGY QHSCTPVFSS IPLLATLQLI EAVGFSNMVE KARRLTGTLE ALLKASRYYV 

       370        380        390        400        410        420 
HPADPKGKIG FKIITPAAPY RGTQLSLVIL PEEEHVMPKV FDRMLRKGLV GDERKPSVIR 

       430        440        450 
LSPVVLYNTF EEVGRAVEIV EEALEEEEEE RKR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEY01000013 Genomic DNA. Translation: EAL22182.1.
RefSeqXP_776829.1. XM_771736.1.

3D structure databases

ProteinModelPortalP0CO53.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4934985.
KEGGcnb:CNBC3200.

Phylogenomic databases

HOGENOMHOG000242438.
KOK01556.
OrthoDBEOG7V1G0J.

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. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_CRYNB
AccessionPrimary (citable) accession number: P0CO53
Secondary accession number(s): Q55W17, Q5KK77
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways