Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynureninase

Gene

BNA5

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
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 sitei145 – 1451Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei146 – 1461Pyridoxal phosphateUniRule annotation
Binding sitei258 – 2581Pyridoxal phosphateUniRule annotation
Binding sitei261 – 2611Pyridoxal phosphateUniRule annotation
Binding sitei283 – 2831Pyridoxal phosphateUniRule annotation
Binding sitei313 – 3131Pyridoxal phosphateUniRule annotation
Binding sitei341 – 3411Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

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:BNA5UniRule annotation
ORF Names:PODANS_7_770Imported
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)Imported
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
ProteomesiUP000001197 Componenti: Chromosome 7

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB2AP14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1764Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

KOiK01556.

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.

B2AP14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSLTAAFRS GQKPSFPAEA GTLEYAQSLD QQDKLGHLRK EFNIPTRTSL
60 70 80 90 100
KKKALNGVSP GENDSEDEKS IYFVGNSLGA QPKAVRRALE SQLETWASIG
110 120 130 140 150
VNGHFSTLEN SPLSSWQDLA ESCARKSVDL VGAAVPEEII YMNTLTANLH
160 170 180 190 200
LMMASFYKPT AERDKVIIEW KPFPSDWYAI QSQIRHHNLS PSTSLIEIQP
210 220 230 240 250
TPDLYLTTES ILATITEHAP STALVLLPGI QYYTGQLLDI KTITAHAHSL
260 270 280 290 300
GIPCVGWDLA HAAGNVPLHL HDWNVDFAVW CTYKYINAGP GSTAGLFLHQ
310 320 330 340 350
KHHSKNLDRL EGWYGADKSV RFLMEKEFKP SKGASGWQLS NPSAIDLASV
360 370 380 390 400
SAALGVFESV GERYMERLRG KAVVLTGYLE CLLEGLIRGG VGRKGEEQAF
410 420 430 440 450
RIITPGNPLE RGTQLSLMLR EGILEGVSKV LAEEGVVCDA RKPDVIRVAP
460 470
VPMYCRFEDV WRFVEIFKGA LARV
Length:474
Mass (Da):52,305
Last modified:May 20, 2008 - v1
Checksum:iDCB0CA4CB24A6003
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633873 Genomic DNA. Translation: CAP65719.1.
FO904942 Genomic DNA. Translation: CDP32779.1.
RefSeqiXP_001905477.1. XM_001905442.1.

Genome annotation databases

GeneIDi6189648.
KEGGipan:PODANSg2503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633873 Genomic DNA. Translation: CAP65719.1.
FO904942 Genomic DNA. Translation: CDP32779.1.
RefSeqiXP_001905477.1. XM_001905442.1.

3D structure databases

ProteinModelPortaliB2AP14.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6189648.
KEGGipan:PODANSg2503.

Phylogenomic databases

KOiK01556.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383Imported and S mat+Imported.
  2. Genoscope - CEA
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: S mat+Imported.
  3. Genoscope - CEA
    Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Maintaining two mating types: Structure of the mating type locus and its role in heterokaryosis in Podospora anserina."
    Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E., Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.
    Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiB2AP14_PODAN
AccessioniPrimary (citable) accession number: B2AP14
Entry historyi
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: April 29, 2015
This is version 52 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.