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Q5BC73 (KYNU2_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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

Names and origin

Protein namesRecommended name:
Kynureninase 2

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene names
Name:bna5-2
ORF Names:AN1857
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 length474 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 caution

The sequence EAA65022.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' NAD biosynthetic process from tryptophan

Inferred from electronic annotation. Source: EnsemblFungi

L-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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: UniProtKB-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 – 474474Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356978

Regions

Region172 – 1754Pyridoxal phosphate binding By similarity

Sites

Binding site1441Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1451Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate By similarity
Binding site2831Pyridoxal phosphate By similarity
Binding site3231Pyridoxal phosphate By similarity
Binding site3511Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2841N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BC73 [UniParc].

Last modified November 16, 2011. Version 2.
Checksum: 12D43A644E6F499F

FASTA47452,467
        10         20         30         40         50         60 
MSNHVNGVNG VNGVNGVKPV FPENAASKEY AKALDAADPL ASFRDKFIIP SKANIQSKRL 

        70         80         90        100        110        120 
AKPNISADPC IYFCGNSLGL QPKATAKYME AHLDTWASIG VNGHFTKIED SPLDPWWVMA 

       130        140        150        160        170        180 
EQAAGSMSKL VGAAPEEVIA MGTLTSNLHL LLASFYKPTA TKHKILLDWK AFPSDHYAIE 

       190        200        210        220        230        240 
SHIAWHDGLD PKKSMVLIGP DEGEYEIPTQ KILSIIDEHA DEAALILLPG IQYYTGQYFD 

       250        260        270        280        290        300 
INTITEYAHS KGLMVGWDLA HAFANVELKL HEWDVDFAVW CTYKYANAGP GSMGGLFVHE 

       310        320        330        340        350        360 
KHGKVDYSQG EDSPQFRHRL AGWYGGDRSV RFKMDNKFRP IPGAGGFQLS TSSATDLTCL 

       370        380        390        400        410        420 
NASLSIFDQT SISELRRKSV QLTAYLEYLL LKDTTDETRP FRIITPSNPE ERGAQLSLLL 

       430        440        450        460        470 
KPGLLQRVAD KLQSASIVCD KREPGVVRVA PAPLYNTYSE VWQFVEQLKA AFQE 

« 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
AACD01000029 Genomic DNA. Translation: EAA65022.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF85703.1.
RefSeqXP_659461.1. XM_654369.1.

3D structure databases

ProteinModelPortalQ5BC73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008511; CADANIAP00008511; CADANIAG00008511.
GeneID2875742.
KEGGani:AN1857.2.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAGWYGGDK.
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 nameKYNU2_EMENI
AccessionPrimary (citable) accession number: Q5BC73
Secondary accession number(s): C8VKF6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 55 of the entry and version 2 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