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Reviewed, UniProtKB/Swiss-Prot A7SCH8 (KYNU_NEMVE)

Last modified November 3, 2009. Version 14. 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
Gene names
Name: kynu
ORF Names: v1g235255
OrganismNematostella vectensis (Starlet sea anemone) [Complete proteome]
Taxonomic identifier45351 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella

Protein attributes

Sequence length465 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 – 465465Kynureninase
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
A7SCH8-1 [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: 17615350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH2 X CH6.

Cross-references

Sequence databases

DS469623 Genomic DNA. Translation: EDO38606.1.
RefSeqXP_001630669.1.
UniGeneNve.12420

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5510175.
KEGGnve:NEMVE_v1g235255.

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_NEMVE
AccessionPrimary (citable) accession number: A7SCH8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 2, 2007
Last modified: November 3, 2009
This is version 14 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

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