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Q4HYR2 (ACEA_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:
Isocitrate lyase

Short name=ICL
Short name=Isocitrase
Short name=Isocitratase
EC=4.1.3.1
Gene names
Name:ICL1
ORF Names:FGSG_09896
OrganismGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum) [Reference proteome]
Taxonomic identifier229533 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaemitosporic NectriaceaeFusarium

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Isocitrate = succinate + glyoxylate.

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.

Subunit structure

Homotetramer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentPeroxisome
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisocitrate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Isocitrate lyase
PRO_0000286157

Sites

Active site2151 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4HYR2 [UniParc].

Last modified August 16, 2005. Version 1.
Checksum: C90BD9BFBAB4BE9D

FASTA54660,826
        10         20         30         40         50         60 
MASQNMTNPS INPDIEDELF QKEVEAVKTW WSDSRWRQTK RPFTAEQIVS KRGYLPIDYA 

        70         80         90        100        110        120 
SNTQAKKLWK ILEHRFENRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASASDEP 

       130        140        150        160        170        180 
GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ RQERLSVPKE QRANLLNIDY LRPIVADADT 

       190        200        210        220        230        240 
GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA 

       250        260        270        280        290        300 
DIMGSDLLAI ARTDAEAATL LSTNIDPRDH AFILGSTNST LKPLNDLMIA AEATGKSGAE 

       310        320        330        340        350        360 
LQRIEDEWLA KANLSSFDDA VAAAIDAGSF SDKAGIKQEY TSRAKGKSNF EARAVARQLL 

       370        380        390        400        410        420 
GRDIFFDWDA PRTREGYFRL KGGCDCAVNR AIAYAPYCDA IWMESKLPDF AQAEQFAQGV 

       430        440        450        460        470        480 
HAVWPEKKLA YNLSPSFNWK TAMPRDEQET YIRRLAKLGY CWQFITLAGL HTTALISDQF 

       490        500        510        520        530        540 
AKAYSTVGMR AYGELVQEPE MDQKVDVVKH QKWSGATYVD ELQKMVTGGI SSTAAMGAGV 


TEDQFK 

« 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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231669 Genomic DNA. Translation: ESU16540.1.
RefSeqXP_390072.1. XM_390072.1.

3D structure databases

ProteinModelPortalQ4HYR2.
SMRQ4HYR2. Positions 16-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5518.FG09896.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFGSG_09896T0; FGSG_09896P0; FGSG_09896.
GeneID2791934.
KEGGfgr:FG09896.1.

Phylogenomic databases

eggNOGCOG2224.
KOK01637.
OrthoDBEOG73Z331.

Enzyme and pathway databases

UniPathwayUPA00703; UER00719.

Family and domain databases

Gene3D3.20.20.60. 2 hits.
InterProIPR006254. Isocitrate_lyase.
IPR000918. Isocitrate_lyase/Pmutase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 1 hit.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR01346. isocit_lyase. 1 hit.
PROSITEPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACEA_GIBZE
AccessionPrimary (citable) accession number: Q4HYR2
Secondary accession number(s): V6RX12
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: August 16, 2005
Last modified: April 16, 2014
This is version 60 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