Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4UBV5 (KYNU_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. 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
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
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene names
Name:BNA5
ORF Names:MGG_10969
OrganismMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]
Taxonomic identifier242507 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe ›

Protein attributes

Sequence length497 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.

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.

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_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mycelium development

Inferred from expression pattern PubMed 17156450. Source: PAMGO_MGG

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 – 497497Kynureninase HAMAP-Rule MF_03017
PRO_0000360870

Regions

Region194 – 1974Pyridoxal phosphate binding By similarity

Sites

Binding site1661Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1671Pyridoxal phosphate By similarity
Binding site2781Pyridoxal phosphate By similarity
Binding site2811Pyridoxal phosphate By similarity
Binding site3031Pyridoxal phosphate By similarity
Binding site3371Pyridoxal phosphate By similarity
Binding site3651Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue3041N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4UBV5 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: F15D53786575CFDB

FASTA49754,479
        10         20         30         40         50         60 
MAATQKSLCA IPADPIEFPA DANTLDYARS EDAKCPIRHM REHFIFPTRA SLKKKALDGR 

        70         80         90        100        110        120 
LPAYPPNHAK PGETATAQNG TSNTNDDNVT PAVYFCGNSL GLQPKATRDH INAQLETWAS 

       130        140        150        160        170        180 
IGVHGHFTSW DNSPLKSWQD MAADCAAQSA SVVGASPDEI AIMNTLTANL HFMMASFYRP 

       190        200        210        220        230        240 
TEKRHKIISE WKPFPSDTYA IASQIQWHGF DTATSLVELH PDENYYISTE KILATIDEHA 

       250        260        270        280        290        300 
ESTALLLLPG IQYWSGQLFD MPLITAHARA KGIVVGWDLA HAVGNVPLSL HDWDVDFAIW 

       310        320        330        340        350        360 
CTYKYLNAGP GAIAGAFVHE RHGKVDSDGF KLRLSGWYGN NKATRFNMAK DFDPTPGAQG 

       370        380        390        400        410        420 
WVVSNPSGID LASLGAALSV YNLTTPADLR KKSLWLTAYA EHLLNGILKD EAASSAGDGK 

       430        440        450        460        470        480 
KPAFRIITPS NKNERGAQLS VLLREGLLDV VGEKMEAAGV VCDRRKPDVM RVAPVPMYNS 

       490 
YEDVWRCVDA LRKAVMS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CM001235 Genomic DNA. Translation: EHA48171.1.
CM001235 Genomic DNA. Translation: EHA48172.1.
RefSeqXP_003717755.1. XM_003717707.1.
XP_003717756.1. XM_003717708.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING148305.A4UBV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2677723.
KEGGmgr:MGG_10969.

Phylogenomic databases

eggNOGCOG3844.
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 nameKYNU_MAGO7
AccessionPrimary (citable) accession number: A4UBV5
Secondary accession number(s): G4NBX0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 25, 2012
Last modified: April 3, 2013
This is version 56 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents