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A7SCH8 (KYNU_NEMVE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynu
ORF Names:v1g235255
OrganismNematostella vectensis (Starlet sea anemone) [Reference proteome]
Taxonomic identifier45351 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella

Protein attributes

Sequence length465 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.

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: UniProtKB-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 – 465465Kynureninase HAMAP-Rule MF_03017
PRO_0000361088

Regions

Region161 – 1644Pyridoxal phosphate binding By similarity

Sites

Binding site1331Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1341Pyridoxal phosphate By similarity
Binding site2171Pyridoxal phosphate By similarity
Binding site2461Pyridoxal phosphate By similarity
Binding site2491Pyridoxal phosphate By similarity
Binding site2711Pyridoxal phosphate By similarity
Binding site3021Pyridoxal phosphate By similarity
Binding site3301Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7SCH8 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 4F52CE41A24A5D9C

FASTA46552,709
        10         20         30         40         50         60 
MAYKPTQTLR KLAEKSSLDI VSREFADYMD SKDPLRKMRD EFFYPRVKDL PGVDLSLVDG 

        70         80         90        100        110        120 
DQDSIYFCGN SLGLQPRGCR ELIDRSLTKW EQMGVLGHTS GWCPWKPIED ILIKPMAEII 

       130        140        150        160        170        180 
GAKDIEVVAM NTLTVNLHMM MVPFYRPTPQ RYKILMEGKA FPSDQYAAQS QVHFHGFDPD 

       190        200        210        220        230        240 
KDIIEVFPRE GEQSLRTEDI LSAIEEHGNS ITLVLFSGVQ YYTGQFFDMK TITAAAQKKG 

       250        260        270        280        290        300 
CVVGWDLAHA VGNVELHLHD WNVDFACWCT YKYLNSGPGG IAGAFVHEKH AYNFELPKFA 

       310        320        330        340        350        360 
GWWGTDRNSR FQMRKEFEQI PGAHGYQCSN PPVFQCLLLR ASLDVFEKTS VKEIRAKGDL 

       370        380        390        400        410        420 
LTAYLELLLL HYFSPSNDIT KNGNTPHVSI ITPADPKDRG CQLSVKFSVP VDKVFEELCK 

       430        440        450        460 
RGFVGDIRHP DVMRIAPAPL YNSFADVHRF ISMLNAAFKT ITPNS 

« Hide

References

[1]"Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization."
Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.
Science 317:86-94(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH2 X CH6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS469623 Genomic DNA. Translation: EDO38606.1.
RefSeqXP_001630669.1. XM_001630619.1.
UniGeneNve.12420.

3D structure databases

ProteinModelPortalA7SCH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING45351.JGI235255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaNEMVEDRAFT_v1g235255-RA; NEMVEDRAFT_v1g235255-PA; NEMVEDRAFT_v1g235255.
GeneID5510175.
KEGGnve:NEMVE_v1g235255.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAWASCEEA.
OrthoDBEOG7D2FDV.

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. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_NEMVE
AccessionPrimary (citable) accession number: A7SCH8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 2, 2007
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways