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Reviewed, UniProtKB/Swiss-Prot A4UBV5 (KYNU_MAGGR)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5
Gene names
Name: BNA5
ORF Names: MGG_10969
OrganismMagnaporthe grisea (Rice blast fungus) (Pyricularia grisea) [Complete proteome]
Taxonomic identifier148305 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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 processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

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 – 510510Kynureninase
PRO_0000360870

Regions

Region207 – 2104Pyridoxal phosphate binding By similarity

Sites

Binding site1791Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1801Pyridoxal phosphate By similarity
Binding site2911Pyridoxal phosphate By similarity
Binding site2941Pyridoxal phosphate By similarity
Binding site3161Pyridoxal phosphate By similarity
Binding site3501Pyridoxal phosphate By similarity
Binding site3781Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue3171N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4UBV5-1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 6327C915CE6E527B

FASTA51055,892
        10         20         30         40         50         60 
MAATQKSLCA IPADPIEFPA DANTLDYARS EDAKCPIRHM REHFIFPTRA SLKKKALDGR 

        70         80         90        100        110        120 
LPVNFELSGP MLDPIAYPPN HAKPGETATA QNGTSNTNDD NVTPAVYFCG NSLGLQPKAT 

       130        140        150        160        170        180 
RDHINAQLET WASIGVHGHF TSWDNSPLKS WQDMAADCAA QSASVVGASP DEIAIMNTLT 

       190        200        210        220        230        240 
ANLHFMMASF YRPTEKRHKI ISEWKPFPSD TYAIASQIQW HGFDTATSLV ELHPDENYYI 

       250        260        270        280        290        300 
STEKILATID EHAESTALLL LPGIQYWSGQ LFDMPLITAH ARAKGIVVGW DLAHAVGNVP 

       310        320        330        340        350        360 
LSLHDWDVDF AIWCTYKYLN AGPGAIAGAF VHERHGKVDS DGFKLRLSGW YGNNKATRFN 

       370        380        390        400        410        420 
MAKDFDPTPG AQGWVVSNPS GIDLASLGAA LSVYNLTTPA DLRKKSLWLT AYAEHLLNGI 

       430        440        450        460        470        480 
LKDEAASSAG DGKKPAFRII TPSNKNERGA QLSVLLREGL LDVVGEKMEA AGVVCDRRKP 

       490        500        510 
DVMRVAPVPM YNSYEDVWRC VDALRKAVMS 

« Hide

Cross-references

Sequence databases

DS231523 Genomic DNA. Translation: EDK06606.1.
RefSeqXP_361892.1.
UniGeneMgr.14510

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2677723.
KEGGmgr:MGG_10969.
NMPDRfig|242507.1.peg.3632.

Phylogenomic databases

OMAWQPLSGW.

Family and domain databases

InterProIPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_MAGGR
AccessionPrimary (citable) accession number: A4UBV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 15, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents