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A5DM91 (KYNU_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PGUG_04392
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Meyerozyma ›

Protein attributes

Sequence length445 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

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 – 445445Kynureninase HAMAP-Rule MF_03017
PRO_0000360871

Regions

Region132 – 1354Pyridoxal phosphate binding By similarity

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1051Pyridoxal phosphate By similarity
Binding site2161Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2411Pyridoxal phosphate By similarity
Binding site2761Pyridoxal phosphate By similarity
Binding site3041Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2421N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5DM91 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: C0B61477246C40C5

FASTA44550,662
        10         20         30         40         50         60 
MSAQLDKEYP TFRHLFEVPT LKSLNISSDT NESIYLCGNS LGLMPKSTRK AINDELDTWA 

        70         80         90        100        110        120 
QQGVEGHFSH PERTPWVDID LPLLPLMAPI VGAKESEVAV MGSLTSNLNA MLMSFYKPKG 

       130        140        150        160        170        180 
KRTKILFEKH AFPSDYYAFL NIVQLFGYDE SHLIQVAVQD GATYLRTEDI IFEIENNAEE 

       190        200        210        220        230        240 
LALVCFPGIQ YYTGQFFDIK SITKAAQDHG ICVGWDLAHA VGNVPLNLHD WNVDFAVWCS 

       250        260        270        280        290        300 
YKYLNSGPGA MAGIFVHQRH TENNSKTSYN PRLAGWWGNN AQERFQMKEE FNPINSALSY 

       310        320        330        340        350        360 
RQSNPSVIDT VAVKASLKVF QEANGIQFLR EKSIKMTQFL QDLLTQSQYY INQNEKPTKL 

       370        380        390        400        410        420 
GFQILTPLDP NQRGCQLSLL FHPHYDEKSK NIMEQVNKYL HNRGIVCDER RPDVIRVAPT 

       430        440 
PLYNTFAEIE YAVKSLNEAL NQIEN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH408159 Genomic DNA. Translation: EDK40294.2.
RefSeqXP_001483663.1. XM_001483613.1.

3D structure databases

ProteinModelPortalA5DM91.
ModBaseSearch...

Protein-protein interaction databases

STRING4929.A5DM91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5125646.
KEGGpgu:PGUG_04392.

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_PICGU
AccessionPrimary (citable) accession number: A5DM91
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 22, 2008
Last modified: April 3, 2013
This is version 38 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

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