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Q4X1D4 (KYNU1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. 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 1
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene names
Name:bna5-1
ORF Names:AFUA_2G10360
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length509 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
Reference proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

de novo NAD biosynthetic process from tryptophan

Inferred from electronic annotation. Source: EnsemblFungi

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 – 509509Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356965

Regions

Region197 – 2004Pyridoxal phosphate binding By similarity

Sites

Binding site1691Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1701Pyridoxal phosphate By similarity
Binding site2831Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3081Pyridoxal phosphate By similarity
Binding site3491Pyridoxal phosphate By similarity
Binding site3771Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue3091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4X1D4 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: FAB6BF3A24F37D13

FASTA50957,148
        10         20         30         40         50         60 
MGSRLHVQVI HGGPPLPYKD DIRAFGKEYA EQLDAQDPLR RFRDEFIIPS KKDLKRKTLF 

        70         80         90        100        110        120 
PNDGMYSCGH PICFANTSCA CVHAAETEET SDEKCIYLCG NSLGLQPRST RKYIDHYLRT 

       130        140        150        160        170        180 
WATKGVTGHF VPHDDQLLPP FVDVDEAGAK LMAPIVGALK SEVAVMGTLT ANLHLLMASF 

       190        200        210        220        230        240 
YRPTPERNKI IIEGKAFPSD HYAVESQIRH HNLDPKDAMV LIEPEDLDRP ILDTKYILRV 

       250        260        270        280        290        300 
IDENAHSTAL ILLPAIQFYT GQYFDIQRIT AHAQSKGILV GWDCAHAAGN VDLRLHDWNV 

       310        320        330        340        350        360 
DFAAWCTYKY LNAGPGGMAA LFVHERHGRV DIEQAASGKE AFHPRFSGWW GGDKQTRFLM 

       370        380        390        400        410        420 
NNHFVPQQGA AGFQLSNPSV LDMNAVVASL ELFNQTSMAE IRKKSLNLTG YLEHLLLRDP 

       430        440        450        460        470        480 
QTENSEKRPF SIITPSNPAE RGAQLSIRLQ PGLLDRVLES LNEDAVIIDE RKPDVIRVAP 

       490        500 
APLYNTYAEV WRFAQLFHLA CDKALCGRK

« 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] [Europe PMC] [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		AAHF01000001 Genomic DNA. Translation: EAL93331.1.
RefSeqXP_755369.1. XM_750276.1.

3D structure databases

ProteinModelPortalQ4X1D4.
ModBaseSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00004107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00004107; CADAFUAP00004107; CADAFUAG00004107.
GeneID3512699.
KEGGafm:AFUA_2G10360.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMADERKPDV.
OrthoDBEOG4TB7KQ.

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 nameKYNU1_ASPFU
AccessionPrimary (citable) accession number: Q4X1D4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 5, 2005
Last modified: May 1, 2013
This is version 59 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

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