Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4WPN0 (KYNU2_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 49. 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
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 2
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene names
Name:bna5-2
ORF Names:AFUA_4G09840
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length464 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
Reference 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 – 464464Kynureninase 2
PRO_0000356966

Regions

Region163 – 1664Pyridoxal phosphate binding By similarity

Sites

Binding site1351Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1361Pyridoxal phosphate By similarity
Binding site2481Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site3131Pyridoxal phosphate By similarity
Binding site3411Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WPN0 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 4143524AE1667152

FASTA46451,198
        10         20         30         40         50         60 
MSTNGTLSKP EFPANAASKE YAASLDAADP FAGFREKFII PSKANIASTK LAKPGLSSEP 

        70         80         90        100        110        120 
CIYFCGNSLG IQPKATQKYL EAQLDTWSSI GVCGHFTKIE DSPLKEWQNL AEQAAESMSK 

       130        140        150        160        170        180 
IVGAAPEEVA AMGTLTMNLH LLLASFFKPT ATKRKILMDW KAFPSDHYAI ESHLAWHHLD 

       190        200        210        220        230        240 
PKETMVLIGP DEGTYEIPTE KILSYIDQHA DEAALILLPG IQYYTGQLFD IPKITEYAHS 

       250        260        270        280        290        300 
RGLIVGWDLA HAYANVPLKL HDWDVDFAAW CTYKYGNAGP GAMAGLFVHE KHGQVDYSEG 

       310        320        330        340        350        360 
EDAPKFRHRL TGWYGGDKSV RFKMDNKFKP IPGAGGYQIS NPSAIDLACL CAALSVFDET 

       370        380        390        400        410        420 
SIAELRKKSV LMTAYLEYLL LKDTTDESRQ FQIITPSDPA ARGAQLSLLL KPGLLHKVAH 

       430        440        450        460 
RLQEAGIICD KREPGVVRVA PVPLYNTFTE IWMFVQQLKA ALEG

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000005 Genomic DNA. Translation: EAL89804.1.
RefSeqXP_751842.1. XM_746749.1.

3D structure databases

ProteinModelPortalQ4WPN0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WPN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00008333; CADAFUAP00008333; CADAFUAG00008333.
GeneID3509348.
GenomeReviewsGene locus bna5-2 in contig CM000172_GR.
KEGGafm:AFUA_4G09840.

Phylogenomic databases

eggNOGfuNOG06509.
GeneTreeEFGT00050000005118.
HOGENOMHBG523016.
OMAGVFVHEK.
OrthoDBEOG4TB7KQ.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01556.
PANTHERPTHR14084. Kynureninase. 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 nameKYNU2_ASPFU
AccessionPrimary (citable) accession number: Q4WPN0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 5, 2005
Last modified: December 14, 2011
This is version 49 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents