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I1RLM3 (I1RLM3_GIBZE) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 HAMAP-Rule MF_03017

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_03017

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity PIRNR PIRNR038800 HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region189 – 1924Pyridoxal phosphate binding By similarity HAMAP-Rule MF_03017

Sites

Binding site1611Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_03017
Binding site1621Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2731Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2761Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2981Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3381Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3661Pyridoxal phosphate By similarity HAMAP-Rule MF_03017

Amino acid modifications

Modified residue2991N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_03017

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]"Genome Sequence of Fusarium graminearum (Gibberella zeae)."
The Broad Institute Genome Sequencing Platform
Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D. expand/collapse author list , Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Kistler C., Xu J.-R., Trail F.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PH-1 EMBL ESU10704.1.
[3]"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., Chapman S., Coulson R., Coutinho P.M., Danchin E.G., 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.
[4]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

EMBL
GenBank
DDBJ
DS231665 Genomic DNA. Translation: ESU10704.1.
RefSeqXP_385005.1. XM_385005.1.

3D structure databases

ProteinModelPortalI1RLM3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

KOK01556.
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. 2 hits.
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: July 9, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)