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A9V3C0 (KYNU_MONBE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 36. 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
EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynu
ORF Names:26773
OrganismMonosiga brevicollis (Choanoflagellate) [Reference proteome]
Taxonomic identifier81824 [NCBI]
Taxonomic lineageEukaryota › Choanoflagellida › Codonosigidae › Monosiga

Protein attributes

Sequence length460 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
Reference 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 – 460460Kynureninase HAMAP-Rule MF_03017
PRO_0000361087

Regions

Region165 – 1684Pyridoxal phosphate binding By similarity

Sites

Binding site1271Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1281Pyridoxal phosphate By similarity
Binding site2491Pyridoxal phosphate By similarity
Binding site2521Pyridoxal phosphate By similarity
Binding site2741Pyridoxal phosphate By similarity
Binding site3041Pyridoxal phosphate By similarity
Binding site3321Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2751N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9V3C0 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8ED7320A036A9BDE

FASTA46051,259
        10         20         30         40         50         60 
MHLARELGVN LADQRLAQAL DEADPLAHLR QEFSIPQMKD IKQADLKLVE AESDCIYLCG 

        70         80         90        100        110        120 
NSLGLMPKRT RTIVNEELDT WATGGVTGHF PDGPGKRPWV SIDETVTDKC ARVVGALPEE 

       130        140        150        160        170        180 
VAIMNTLTVN LHLLMVSLAH TMARQVPFYR PTSDRFKILV EAKAFPSDHF AVLSQLRMHG 

       190        200        210        220        230        240 
HDESALIEVK PREGEHNIRE EDLLAILEEQ GDSIATVLVG GVHYYTGQFF DLQRLCAAAH 

       250        260        270        280        290        300 
NKGCTFGVDL AHAVGNVPLQ LHDWDIDFAC WCTYKYLNSG PGGIAGAFIH KKHEGTSRPY 

       310        320        330        340        350        360 
LQGWWGVQLN ERFRMDHDAS FMPGVRGLQL SNPGVLQTVA LLGSLEIYEQ TDMASLRAKS 

       370        380        390        400        410        420 
LKLTAYLEQL MQALVNEEGH APRFEIITPT DPERRGCQLS ILFKVDIDAA FEALEKRGVV 

       430        440        450        460 
CDVRRPDVMR IAPVPLYNTF TDVYRFVTTL RDALNASASS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH991556 Genomic DNA. Translation: EDQ88034.1.
RefSeqXP_001747110.1. XM_001747058.1.

3D structure databases

ProteinModelPortalA9V3C0.
SMRA9V3C0. Positions 3-456.
ModBaseSearch...

Protein-protein interaction databases

STRING81824.JGI26773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5892477.
KEGGmbr:MONBRDRAFT_26773.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAMLTHVNY.
ProtClustDBCLSZ2430281.

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_MONBE
AccessionPrimary (citable) accession number: A9V3C0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 5, 2008
Last modified: April 3, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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