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I1RLM3 (I1RLM3_GIBZE) Unreviewed, UniProtKB/TrEMBL

Last modified March 6, 2013. Version 8. Feed History...

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

Protein attributes

Sequence length491 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. PIRNR PIRNR038800

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800

Subcellular location

Cytoplasm By similarity PIRNR PIRNR038800.

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800

Sequences

Sequence LengthMass (Da)Tools
I1RLM3 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 858E6BA7996A792A

FASTA49154,235
        10         20         30         40         50         60 
MELSSFVERL RSSAPPKFPS DANSLDFARN LDSQDKLSHL RDEFILPTKK SLKKKALDGS 

        70         80         90        100        110        120 
IPNGHAQNGS VNGTNGHTNG QDDDQQCIYF VGNSLGAQPK AVREHLNAQL ETWASVGVNG 

       130        140        150        160        170        180 
HFSAMGNSPL PAWQDLAEDC AIRSADIVGA SPHEIVIMNT LTANLHLLMA SFYKPNEKRH 

       190        200        210        220        230        240 
KVILEWKPFP SDHYAIESQV VWHGLDPEKS MVKIEPNEDH IITTDLILST IDQHADDTAL 

       250        260        270        280        290        300 
LLLPGIQYYS GQLFDIPRIT AYAQAKGIVV GWDLAHAAGN VELKLHDWNV DFACWCTYKY 

       310        320        330        340        350        360 
INAGPGSIAG AYVHERHGKV EMNSETGKAS YRPRLMGWYG GDKSVRFNMD NNFIPTAGAG 

       370        380        390        400        410        420 
GFQLSNPSAI DLASLSGALS VFNKTTMHDL RSKALVLTAY SEYLLDQILS ESGDSELFRI 

       430        440        450        460        470        480 
ITPRDPLQRG TQLSVLLKDG LLDNVSAALE ENAVICDKRK PGVIRVAPVP LYSRFEDVWR 

       490 
FMQILRGALK N

« Hide

References

« Hide 'large scale' references
[1]"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization."
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. expand/collapse author list , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.
Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084 EnsemblFungi FGSG_04829P0.
[2]"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. expand/collapse author list , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084 EnsemblFungi FGSG_04829P0.
[3]EnsemblFungi
Submitted (OCT-2012) to UniProtKB
Cited for: IDENTIFICATION.
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084 EnsemblFungi FGSG_04829P0.

Cross-references

Sequence databases

RefSeqXP_385005.1. XM_385005.1.

3D structure databases

ProteinModelPortalI1RLM3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFGSG_04829T0; FGSG_04829P0; FGSG_04829.
GeneID2786459.
KEGGfgr:FG04829.1.

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameI1RLM3_GIBZE
AccessionPrimary (citable) accession number: I1RLM3
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: March 6, 2013
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info