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Q7RXY2 (KYNU2_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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:kyn-2
Synonyms:bna5-2
ORF Names:NCU00463
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length472 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000218663

Regions

Region162 – 1654Pyridoxal phosphate binding By similarity

Sites

Binding site1331Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1341Pyridoxal phosphate By similarity
Binding site2471Pyridoxal phosphate By similarity
Binding site2501Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate By similarity
Binding site3141Pyridoxal phosphate By similarity
Binding site3421Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7RXY2 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 8BEAFE163C96995C

FASTA47251,627
        10         20         30         40         50         60 
MSTAAVQDAR KQAEALDNED SIAFVRDEFN IPTKAQIASS RLADSHPAAL PASEDDAKCI 

        70         80         90        100        110        120 
YLCGNSLGVQ PKRTVTRLNQ YLTTWATQGV QGHFKPLEES PLPTWLDADA KAAELIAPVV 

       130        140        150        160        170        180 
GANVSEVAVM QTLTANIHLL MSAFYRPDIN GRHKIILENK AFPSDHFAVE TQIRHHSLST 

       190        200        210        220        230        240 
EKSMVLIESS SKDNIISTEE VLSVISAHAD TTALLLLPGI QYYTGQLLDI PAITAFAHKH 

       250        260        270        280        290        300 
GIFVIWDLAH AVGNVPLYLH DWGVDAAAWC SYKYLNGGPG CIGGLFVHTN NSVVTKEITD 

       310        320        330        340        350        360 
EKPEEGYNNR LAGWWGNDKK TRFVMANKFH PVAGAAGFQL SNPSILDITS LSASLEIFQE 

       370        380        390        400        410        420 
AGGMEALRSK SLKLTSFLEA TLGHMKEEDR AHFRIITPSK SEERGAQLSL MLSDGLLDTV 

       430        440        450        460        470 
MKELEARGVI VDERKPNVIR VAPAPLYNTF KDCVLFVEAF SAALEVAKQH AL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM002238 Genomic DNA. Translation: EAA27546.2.
RefSeqXP_956782.2. XM_951689.2.
UniGeneNcr.4495.

3D structure databases

ProteinModelPortalQ7RXY2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU00463.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000000064; EFNCRP00000000064; EFNCRG00000000064.
GeneID3872929.
KEGGncr:NCU00463.

Phylogenomic databases

eggNOGCOG3844.
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 nameKYNU2_NEUCR
AccessionPrimary (citable) accession number: Q7RXY2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: December 4, 2007
Last modified: June 11, 2014
This is version 78 of the entry and version 2 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