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A1DGW4 (KYNU1_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 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:NFIA_085760
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya ›

Protein attributes

Sequence length487 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

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 – 487487Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356979

Regions

Region175 – 1784Pyridoxal phosphate binding By similarity

Sites

Binding site1471Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1481Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3271Pyridoxal phosphate By similarity
Binding site3551Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2871N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1DGW4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 831F18F1EC3CAAC7

FASTA48755,160
        10         20         30         40         50         60 
MGSRLHVQEI QGGPPLPYED DIRAFCKEYA ELLDAHDPLR RFRDEFIVPS KKDLKRKTLF 

        70         80         90        100        110        120 
PNDETEETSD EECIYLCGNS LGLQPRSTRK YIEYYLRTWA TKGVTGHFVP HDDQLLPPFV 

       130        140        150        160        170        180 
NVDEAGAKLM APIVGALKSE VAVMGTLTAN LHLLMASFYR PTRERYKIII EGKAFPSDHY 

       190        200        210        220        230        240 
AVESQIRHHN LDPKDAMVLI ESDDLDRPIL DTEYILRVID ENAHSTALIL LSAIQFYTGQ 

       250        260        270        280        290        300 
YFDIQRITAH AQSKGILVGW DCAHAAGNVD LRLHDWNVDF AAWCTYKYLN AGPGGMAALF 

       310        320        330        340        350        360 
VHERHGRVDM EQAASGKEAF HPRFSGWWGG DKQTRFLMNN HFVPQQGAAG FQLSNPSVLD 

       370        380        390        400        410        420 
MNAVVASLEL FNQTSMAEIR KKSLNLTGYL EHLLLRDPQT ESSEKRPFSI ITPSNPAERG 

       430        440        450        460        470        480 
AQLSIRLQPG LLDRVLESLD EDAVIIDERK PDVIRVAPAP LYNTYVEVWR FAQLFHLACD 


KALRGRE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DS027696 Genomic DNA. Translation: EAW18621.1.
RefSeqXP_001260518.1. XM_001260517.1.

3D structure databases

ProteinModelPortalA1DGW4.
ModBaseSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00006511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00006678; CADNFIAP00006511; CADNFIAG00006678.
GeneID4587076.
KEGGnfi:NFIA_085760.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
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_NEOFI
AccessionPrimary (citable) accession number: A1DGW4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 40 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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