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A1CWY1 (KYNU2_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 47. 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 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:NFIA_106210
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

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. 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356980

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
A1CWY1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 068410138459920C

FASTA46451,232
        10         20         30         40         50         60 
MSTNGTLSKP EFPANAASKE YAASLDAADP LAGFREKFII PSKANIASTK LAKPGLSSEP 

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

       130        140        150        160        170        180 
IVGAAPDEVA AMGTLTMNLH LLLASFYKPT ATKRKILMDW KAFPSDHYAI ESHVAWHHLD 

       190        200        210        220        230        240 
PQETMVLIGP DEGTYEIPTE KILSYIDTHA DEAALILLPG IQYYTGQLFD IPKITEYAHS 

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

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

       370        380        390        400        410        420 
SMAELRKKSV LMTAYLEYLL LKDTTDESRQ FQIVTPSDPA ARGAQLSLLL KPGLLHKVAH 

       430        440        450        460 
RLQEAGIICD KREPGVVRVA PVPLYNTFTE IWMFVQQLKA ALEE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027685 Genomic DNA. Translation: EAW25133.1.
RefSeqXP_001267030.1. XM_001267029.1.

3D structure databases

ProteinModelPortalA1CWY1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00009440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00009680; CADNFIAP00009440; CADNFIAG00009680.
GeneID4594082.
KEGGnfi:NFIA_106210.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAGWYGGDK.
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 nameKYNU2_NEOFI
AccessionPrimary (citable) accession number: A1CWY1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 47 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