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Protein

Kynureninase

Gene

FG04829.1

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Status
Unreviewed-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-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei161 – 1611Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei162 – 1621Pyridoxal phosphateUniRule annotation
Binding sitei273 – 2731Pyridoxal phosphateUniRule annotation
Binding sitei276 – 2761Pyridoxal phosphateUniRule annotation
Binding sitei298 – 2981Pyridoxal phosphateUniRule annotation
Binding sitei338 – 3381Pyridoxal phosphateUniRule annotation
Binding sitei366 – 3661Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Pyridine nucleotide biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

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):
Biosynthesis of nicotinic acid protein 5UniRule annotation
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:FG04829.1Imported
Synonyms:BNA5UniRule annotation
ORF Names:FGSG_04829Imported
OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)Imported
Taxonomic identifieri229533 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
ProteomesiUP000009057: Chromosome 3

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliI1RLM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

KOiK01556.
OrthoDBiEOG7V1G0J.

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. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

I1RLM3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELSSFVERL RSSAPPKFPS DANSLDFARN LDSQDKLSHL RDEFILPTKK
60 70 80 90 100
SLKKKALDGS IPNGHAQNGS VNGTNGHTNG QDDDQQCIYF VGNSLGAQPK
110 120 130 140 150
AVREHLNAQL ETWASVGVNG HFSAMGNSPL PAWQDLAEDC AIRSADIVGA
160 170 180 190 200
SPHEIVIMNT LTANLHLLMA SFYKPNEKRH KVILEWKPFP SDHYAIESQV
210 220 230 240 250
VWHGLDPEKS MVKIEPNEDH IITTDLILST IDQHADDTAL LLLPGIQYYS
260 270 280 290 300
GQLFDIPRIT AYAQAKGIVV GWDLAHAAGN VELKLHDWNV DFACWCTYKY
310 320 330 340 350
INAGPGSIAG AYVHERHGKV EMNSETGKAS YRPRLMGWYG GDKSVRFNMD
360 370 380 390 400
NNFIPTAGAG GFQLSNPSAI DLASLSGALS VFNKTTMHDL RSKALVLTAY
410 420 430 440 450
SEYLLDQILS ESGDSELFRI ITPRDPLQRG TQLSVLLKDG LLDNVSAALE
460 470 480 490
ENAVICDKRK PGVIRVAPVP LYSRFEDVWR FMQILRGALK N
Length:491
Mass (Da):54,235
Last modified:June 13, 2012 - v1
Checksum:i858E6BA7996A792A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231665 Genomic DNA. Translation: ESU10704.1.
RefSeqiXP_385005.1. XM_385005.1.

Genome annotation databases

EnsemblFungiiFGSG_04829T0; FGSG_04829P0; FGSG_04829.
GeneIDi2786459.
KEGGifgr:FG04829.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231665 Genomic DNA. Translation: ESU10704.1.
RefSeqiXP_385005.1. XM_385005.1.

3D structure databases

ProteinModelPortaliI1RLM3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiFGSG_04829T0; FGSG_04829P0; FGSG_04829.
GeneIDi2786459.
KEGGifgr:FG04829.1.

Phylogenomic databases

KOiK01556.
OrthoDBiEOG7V1G0J.

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. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PH-1Imported.
  3. "Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
    Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E.
    , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
    Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.
  4. EnsemblFungi
    Submitted (OCT-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084Imported.

Entry informationi

Entry nameiI1RLM3_GIBZE
AccessioniPrimary (citable) accession number: I1RLM3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: February 4, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.