Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5B0H8 (KYNU1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase 1
EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene names
Name:bna5-1
ORF Names:AN5952
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

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

Cofactor

Pyridoxal phosphate By similarity.

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 2/3.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Kynureninase 1
PRO_0000356977

Regions

Region177 – 1804Pyridoxal phosphate binding By similarity

Sites

Binding site1491Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1501Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate By similarity
Binding site2661Pyridoxal phosphate By similarity
Binding site2881Pyridoxal phosphate By similarity
Binding site3291Pyridoxal phosphate By similarity
Binding site3571Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2891N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5B0H8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 0E77B19E6DCFE55D

FASTA48754,517
        10         20         30         40         50         60 
MGSRLHVQQI KNGPPLPYKD DIRAFTRDYA ASLDAQDPLS HFREEFIIPS VKDLKRKTLD 

        70         80         90        100        110        120 
PSEGEYSSMY LDARCIYLCG NSLGLQPRNT KKYINYYLRT WAIKGVTGHF THHDDELLPP 

       130        140        150        160        170        180 
FVDVDSAGAK LMAPVVGALE SEVAVMGSLT TNLHLLMASF YRPTTERYKI IIEGKAFPSD 

       190        200        210        220        230        240 
HYAVESQIKH HNLQPKDAMV LIEPQDPEHP ILETDRILRV IDEHASTTAL LLLSAIQYYT 

       250        260        270        280        290        300 
GQYFNIEKIT AHAQSKGIVV GWDCAHAAGN VDLKLHDWNV DFAAWCNYKY LNSGPGGMAG 

       310        320        330        340        350        360 
IFVHEKHGEV KAGQGDGELE LFRPRLSGWW GGDKATRFLM DNHFVPQSGA AGYQLSNPSV 

       370        380        390        400        410        420 
LDMNAVVASL ELFNRTSMAE IRQKSLNLTG YLEHLLLASL DGVSDKPFSI ITPPNPSERG 

       430        440        450        460        470        480 
AQLSLRLAPG LLDSVLETLE EYAVVIDERK PDVIRVAPAP LYNTYEEVWQ FCQIFSEACR 


KALEKKD

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000101 Genomic DNA. Translation: EAA57815.1.
BN001301 Genomic DNA. Translation: CBF70497.1.
RefSeqXP_663556.1. XM_658464.1.

3D structure databases

ProteinModelPortalQ5B0H8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5B0H8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00007075; CADANIAP00007075; CADANIAG00007075.
GeneID2870933.
KEGGani:AN5952.2.

Phylogenomic databases

OMATAEAHKR.
OrthoDBEOG4TB7KQ.
PhylomeDBQ5B0H8.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01556.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. Kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU1_EMENI
AccessionPrimary (citable) accession number: Q5B0H8
Secondary accession number(s): C8V3G6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents