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Protein

Kynureninase

Gene

BNA5

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
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.

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate

Pathwayi: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (BNA5)
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.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
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)DescriptionActionsGraphical viewLength
Binding sitei166Pyridoxal phosphate; via amide nitrogen1
Binding sitei167Pyridoxal phosphate1
Binding sitei278Pyridoxal phosphate1
Binding sitei281Pyridoxal phosphate1
Binding sitei303Pyridoxal phosphate1
Binding sitei337Pyridoxal phosphate1
Binding sitei365Pyridoxal phosphate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynureninase (EC:3.7.1.3)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase
Gene namesi
Name:BNA5
ORF Names:MGG_10969
OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic identifieri242507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe
Proteomesi
  • UP000009058 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiFungiDB:MGG_10969.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003608701 – 497KynureninaseAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei304N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi318829.MGG_10969T0.

Structurei

3D structure databases

SMRiA4UBV5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 197Pyridoxal phosphate binding4

Sequence similaritiesi

Belongs to the kynureninase family.

Phylogenomic databases

InParanoidiA4UBV5.
KOiK01556.
OrthoDBiEOG092C20ON.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01970. Kynureninase. 1 hit.
InterProiView protein in InterPro
IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_sub2.
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiView protein in Pfam
PF00266. Aminotran_5. 1 hit.
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

A4UBV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATQKSLCA IPADPIEFPA DANTLDYARS EDAKCPIRHM REHFIFPTRA
60 70 80 90 100
SLKKKALDGR LPAYPPNHAK PGETATAQNG TSNTNDDNVT PAVYFCGNSL
110 120 130 140 150
GLQPKATRDH INAQLETWAS IGVHGHFTSW DNSPLKSWQD MAADCAAQSA
160 170 180 190 200
SVVGASPDEI AIMNTLTANL HFMMASFYRP TEKRHKIISE WKPFPSDTYA
210 220 230 240 250
IASQIQWHGF DTATSLVELH PDENYYISTE KILATIDEHA ESTALLLLPG
260 270 280 290 300
IQYWSGQLFD MPLITAHARA KGIVVGWDLA HAVGNVPLSL HDWDVDFAIW
310 320 330 340 350
CTYKYLNAGP GAIAGAFVHE RHGKVDSDGF KLRLSGWYGN NKATRFNMAK
360 370 380 390 400
DFDPTPGAQG WVVSNPSGID LASLGAALSV YNLTTPADLR KKSLWLTAYA
410 420 430 440 450
EHLLNGILKD EAASSAGDGK KPAFRIITPS NKNERGAQLS VLLREGLLDV
460 470 480 490
VGEKMEAAGV VCDRRKPDVM RVAPVPMYNS YEDVWRCVDA LRKAVMS
Length:497
Mass (Da):54,479
Last modified:January 25, 2012 - v2
Checksum:iF15D53786575CFDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM001235 Genomic DNA. Translation: EHA48171.1.
CM001235 Genomic DNA. Translation: EHA48172.1.
RefSeqiXP_003717755.1. XM_003717707.1.
XP_003717756.1. XM_003717708.1.

Genome annotation databases

EnsemblFungiiMGG_10969T1; MGG_10969T1; MGG_10969.
GeneIDi2677723.
KEGGimgr:MGG_10969.

Entry informationi

Entry nameiKYNU_MAGO7
AccessioniPrimary (citable) accession number: A4UBV5
Secondary accession number(s): G4NBX0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 25, 2012
Last modified: November 22, 2017
This is version 77 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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