Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B2AP14

- B2AP14_PODAN

UniProt

B2AP14 - B2AP14_PODAN

Protein

Kynureninase

Gene

BNA5

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (20 May 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 phosphate.UniRule 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

    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

    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: Chromosome 7

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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/Cys_dSase.
    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

    MDSLTAAFRS GQKPSFPAEA GTLEYAQSLD QQDKLGHLRK EFNIPTRTSL    50
    KKKALNGVSP GENDSEDEKS IYFVGNSLGA QPKAVRRALE SQLETWASIG 100
    VNGHFSTLEN SPLSSWQDLA ESCARKSVDL VGAAVPEEII YMNTLTANLH 150
    LMMASFYKPT AERDKVIIEW KPFPSDWYAI QSQIRHHNLS PSTSLIEIQP 200
    TPDLYLTTES ILATITEHAP STALVLLPGI QYYTGQLLDI KTITAHAHSL 250
    GIPCVGWDLA HAAGNVPLHL HDWNVDFAVW CTYKYINAGP GSTAGLFLHQ 300
    KHHSKNLDRL EGWYGADKSV RFLMEKEFKP SKGASGWQLS NPSAIDLASV 350
    SAALGVFESV GERYMERLRG KAVVLTGYLE CLLEGLIRGG VGRKGEEQAF 400
    RIITPGNPLE RGTQLSLMLR EGILEGVSKV LAEEGVVCDA RKPDVIRVAP 450
    VPMYCRFEDV WRFVEIFKGA LARV 474
    Length:474
    Mass (Da):52,305
    Last modified:May 20, 2008 - v1
    Checksum:iDCB0CA4CB24A6003
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU633873 Genomic DNA. Translation: CAP65719.1.
    RefSeqiXP_001905477.1. XM_001905442.1.

    Genome annotation databases

    GeneIDi6189648.
    KEGGipan:PODANSg2503.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU633873 Genomic DNA. Translation: CAP65719.1 .
    RefSeqi XP_001905477.1. XM_001905442.1.

    3D structure databases

    ProteinModelPortali B2AP14.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6189648.
    KEGGi pan:PODANSg2503.

    Phylogenomic databases

    KOi K01556.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01970. Kynureninase.
    InterProi IPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR14084. PTHR14084. 1 hit.
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038800. KYNU. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01814. kynureninase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383Imported.

    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: October 1, 2014
    This is version 45 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