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Q7S332 (KYNU1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:kyn-1
Synonyms:bna5-1
ORF Names:NCU09183
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 length485 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 – 485485Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356981

Regions

Region183 – 1864Pyridoxal phosphate binding By similarity

Sites

Binding site1551Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1561Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate By similarity
Binding site2701Pyridoxal phosphate By similarity
Binding site2921Pyridoxal phosphate By similarity
Binding site3301Pyridoxal phosphate By similarity
Binding site3581Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2931N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7S332 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: CC38185722A45A37

FASTA48554,175
        10         20         30         40         50         60 
MSDFTSKVKV LRDGQKPEFP SNANTLEYAQ SLDAQDELRH FRNEFIIPTR ASLKKKALDG 

        70         80         90        100        110        120 
IIPGTQANGT TTSTDADTPC IYFVGNSLGA QPKAVRHYLE AQLETWASIG VNGHFSSLSN 

       130        140        150        160        170        180 
SPLTPWQDMA ADCAAKSAAI VGAADPSEVV IMNTLTVNLH FMMASFYRPT DKRHKIILEW 

       190        200        210        220        230        240 
RPFPSDWYAF QSQIEWHGLD PEKSIVEMQP DENLYLSTEK ILATIDEHAE DAALLLLPGI 

       250        260        270        280        290        300 
QYYTGQLFDI PRITKYAQER GIVVGWDLAH CAGNVELQLH DWNVDFAVWC TYKYLNGGPG 

       310        320        330        340        350        360 
SMAGAFVHER HGKVDMSLGK PVFKPRLSGW YGADKSVRFN MDKEFQPTPG AQGFQVSNPS 

       370        380        390        400        410        420 
AIDLTSLAAA LSVFNKTSMK DLRSKALVLT AYTEHLLDEI VRRQPEGEEP AFKIITPRDP 

       430        440        450        460        470        480 
LQRGTQLSLL LRDGLMDKVA AALEENGVVC DKRKPNVIRV APVPMYCRFE DVWKFMEIFE 


AAIRG 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM002238 Genomic DNA. Translation: EAA29857.1.
RefSeqXP_959093.1. XM_954000.1.

3D structure databases

ProteinModelPortalQ7S332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU09183.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000009056; EFNCRP00000009038; EFNCRG00000009041.
GeneID3875240.
KEGGncr:NCU09183.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAPKSIRTH.
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. 2 hits.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU1_NEUCR
AccessionPrimary (citable) accession number: Q7S332
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 66 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