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Q5B0H8 (KYNU1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356977

Regions

Region177 – 1804Pyridoxal phosphate binding By similarity

Sites

Binding site1491Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1501Pyridoxal phosphate By similarity
Binding site2341Pyridoxal 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] [Europe PMC] [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] [Europe PMC] [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...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00007075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAGLMNDIV.
OrthoDBEOG7V1G0J.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 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: June 11, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways