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Protein

Kynureninase

Gene

kynu

Organism
Nematostella vectensis (Starlet sea anemone)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (kynu)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (KMO)
  2. Kynureninase (kynu)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (v1g178517)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei134 – 1341Pyridoxal phosphateUniRule annotation
Binding sitei217 – 2171Pyridoxal phosphateUniRule annotation
Binding sitei246 – 2461Pyridoxal phosphateUniRule annotation
Binding sitei249 – 2491Pyridoxal phosphateUniRule annotation
Binding sitei271 – 2711Pyridoxal phosphateUniRule annotation
Binding sitei302 – 3021Pyridoxal phosphateUniRule annotation
Binding sitei330 – 3301Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynuUniRule annotation
ORF Names:v1g235255
OrganismiNematostella vectensis (Starlet sea anemone)
Taxonomic identifieri45351 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella
ProteomesiUP000001593 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465KynureninasePRO_0000361088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi45351.NEMVEDRAFT_v1g235255-PA.

Structurei

3D structure databases

ProteinModelPortaliA7SCH8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 1644Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiA7SCH8.
KOiK01556.
OMAiKENGQNG.
OrthoDBiEOG7D2FDV.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

A7SCH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYKPTQTLR KLAEKSSLDI VSREFADYMD SKDPLRKMRD EFFYPRVKDL
60 70 80 90 100
PGVDLSLVDG DQDSIYFCGN SLGLQPRGCR ELIDRSLTKW EQMGVLGHTS
110 120 130 140 150
GWCPWKPIED ILIKPMAEII GAKDIEVVAM NTLTVNLHMM MVPFYRPTPQ
160 170 180 190 200
RYKILMEGKA FPSDQYAAQS QVHFHGFDPD KDIIEVFPRE GEQSLRTEDI
210 220 230 240 250
LSAIEEHGNS ITLVLFSGVQ YYTGQFFDMK TITAAAQKKG CVVGWDLAHA
260 270 280 290 300
VGNVELHLHD WNVDFACWCT YKYLNSGPGG IAGAFVHEKH AYNFELPKFA
310 320 330 340 350
GWWGTDRNSR FQMRKEFEQI PGAHGYQCSN PPVFQCLLLR ASLDVFEKTS
360 370 380 390 400
VKEIRAKGDL LTAYLELLLL HYFSPSNDIT KNGNTPHVSI ITPADPKDRG
410 420 430 440 450
CQLSVKFSVP VDKVFEELCK RGFVGDIRHP DVMRIAPAPL YNSFADVHRF
460
ISMLNAAFKT ITPNS
Length:465
Mass (Da):52,709
Last modified:October 2, 2007 - v1
Checksum:i4F52CE41A24A5D9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS469623 Genomic DNA. Translation: EDO38606.1.
RefSeqiXP_001630669.1. XM_001630619.1.
UniGeneiNve.12420.

Genome annotation databases

EnsemblMetazoaiEDO38606; EDO38606; NEMVEDRAFT_v1g235255.
GeneIDi5510175.
KEGGinve:NEMVE_v1g235255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS469623 Genomic DNA. Translation: EDO38606.1.
RefSeqiXP_001630669.1. XM_001630619.1.
UniGeneiNve.12420.

3D structure databases

ProteinModelPortaliA7SCH8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi45351.NEMVEDRAFT_v1g235255-PA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiEDO38606; EDO38606; NEMVEDRAFT_v1g235255.
GeneIDi5510175.
KEGGinve:NEMVE_v1g235255.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiA7SCH8.
KOiK01556.
OMAiKENGQNG.
OrthoDBiEOG7D2FDV.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CH2 X CH6.

Entry informationi

Entry nameiKYNU_NEMVE
AccessioniPrimary (citable) accession number: A7SCH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 2, 2007
Last modified: June 24, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.