A0AA38Y293 · A0AA38Y293_9EURO

  • Protein
    Multifunctional fusion protein
  • Gene
    BNA5
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

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.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 1/3.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site105pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site218pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site221pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site274pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site302pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial outer membrane
Molecular FunctionDNA binding
Molecular FunctionFAD binding
Molecular Functionkynureninase activity
Molecular Functionkynurenine 3-monooxygenase activity
Molecular Functionmetal ion binding
Molecular Functionpyridoxal phosphate binding
Molecular Functionsingle-stranded DNA 3'-5' DNA exonuclease activity
Biological Process'de novo' NAD biosynthetic process from tryptophan
Biological Processanthranilate metabolic process
Biological ProcessDNA repair
Biological ProcessL-kynurenine catabolic process
Biological Processquinolinate biosynthetic process
Biological Processtryptophan catabolic process to kynurenine

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Kynureninase
  • EC number
  • Alternative names
    • Biosynthesis of nicotinic acid protein 5
    • L-kynurenine hydrolase
  • Recommended name
    Kynurenine 3-monooxygenase
  • EC number
  • Alternative names
    • Biosynthesis of nicotinic acid protein 4
    • Kynurenine 3-hydroxylase

Gene names

    • Name
      BNA5
    • Synonyms
      BNA4
    • ORF names
      H2204_007229

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • TK_35
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Trichomeriaceae > Knufia

Accessions

  • Primary accession
    A0AA38Y293

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue244N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.
Monomer. Interacts with ssb (via C-terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1053-1208ExoI SH3-like
Domain1211-1333ExoI C-terminal

Sequence similarities

Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,555
  • Mass (Da)
    175,574
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    CE0FB8BDAB4036F1EA4AD87064DF3889
MSDLLSRTHAIALDAADPLRPLRQEFLIPRHGGGEQTYFVGNSLGLQPRGAQAAVQEVMKQWGELAVEGHFTGPTQWLSYHRLVSAQLARVVGALPSEVVAMNTLSVNLHLMMVSFYRPTAERPVILMEAGAFPTDRHAVEAQIRFHGFDPADCLVEVQPDEANGTISMAAIERAIAAHGPRLALVLWPGVQYRSGQAFDLDAITRAARLQGARIGFDLAHSVGNLPLHLHDVAPDFAVWCHYKYLNSGPGAVAGAFVHERHHRDTTLPRFAGWWGHDEATRFQMAPQFQPAVGAESWQLSNPPILGLAPLRASLDLFERAGMESLRSKSLALTGMLDALVRARLPQVLEIVTPAEPERRGCQLSLRVIGGRERGRALFEHLRAIGVLGDWREPDVIRISPTPLYNRYLDVHHFVEEVEAWAVGAGLAGSLLAILLSRQGWRITLYERRGDPRIADYESGRSINLALAERGRNALRQAGVEDEVMARAVMMRGRMVHPREGEPQLQRYGRDDGEVIWSIHRSDLNTTLLELAEQAGAIVHFHRRLHTVDFDAGYARFIDDRDDSPHDIRFDTLVGADGAGSALRAAMNRREPLGEDIAFLDHSYKELEIPPTDDGGFRIERNALHIWPRGHYMCIALPNHEGTFTVTLFLPNQGDPSFATVNTGVQAEALFAREFADTLPLIPNLRADWEQHPPGLLGTLTLERWHQQDRAVLIGDAAHAMVPFHGQGMNCAFEDCVALARHLMAADDLQSAFAAFEAERKPNARAIQQMALENYLEMRDRVADPAFLLQRELEQELQRRWPTRFVPHYTMVTFLHTPYAEALRRTDIQREMLITATAGHDTLDAIDWNALEAQIHSRLPVFLFYDLETFGQDPRRTRIAQYAAIRTDSDLNEIDTPASFFVRPADDLLPSPMATMVTGITPQQALAEGISEAEAFDRINEQLSRPGTCALGYNTLRFDDEFIRYGLFRNFHDPYEREWRNGNSRWDLLDMLRLMHAIRPEGIHWPKREDGATSFRLEHLAEANGVREGDAHEALSDVRATIGMARLFKQSQPRLWDYALKLRDKRFVGSLLDITALKPVLHISMRYPASRLCAAPVLPLAVHPTINNRVIVFDLDGDIDDLLELPAEVIAQRLYLRASELPEGVARVPLKEVHLNKVPGLVAWNHLRADDHARLGLDVAAIEAKVERLRAFAPQLAEKARQVYNQPRAASVSDVDASLYDGFLGAGDKPLLALARTTPPEQLAALEGRFRDPRLPELLFRYRARNHPGSLAPEERERWNAYRRRRLSGEEGMGELNLAQYQQQLDALAAEAPDDVRRATLLQSLRDWGQHLQEDLFKFLRSLALHNDKTWFNDHRQQYEDHVRQPFLRLLGDLQPALTEVSGHFRADTRGVGGSLFRIHRDARFSNDKSPYKIWQGARLFHERRREVAAPSFYVHLQPGESFVGAGLWHPEPETQRRVRHFILDNPGSWKAAAHAPALRRRFDFEETEKLVRPPRGFPADFEFIDDLKHRNWVMWRSLDDATMTGPRLLSTLGKDLAALGPFVDYLCAALDLEF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPDRN010000049
EMBL· GenBank· DDBJ
KAJ9633084.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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