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Protein

Isocitrate lyase

Gene

ICL1

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.By similarity

Catalytic activityi

Isocitrate = succinate + glyoxylate.By similarity
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.By similarity

Cofactori

Mg2+By similarity

Pathway: glyoxylate cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from isocitrate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Isocitrate lyase (ICL1)
  2. Malate synthase (FGSG_08700)
This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771MagnesiumBy similarity
Active sitei215 – 2151Proton acceptorBy similarity
Binding sitei252 – 2521SubstrateBy similarity
Binding sitei466 – 4661SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyaseBy similarity (EC:4.1.3.1By similarity)
Short name:
ICLCurated
Short name:
IsocitraseCurated
Short name:
IsocitrataseCurated
Alternative name(s):
Methylisocitrate lyaseBy similarity (EC:4.1.3.30By similarity)
Short name:
MICACurated
Threo-D(S)-isocitrate glyoxylate-lyaseCurated
Gene namesi
Name:ICL1By similarity
ORF Names:FGSG_09896
OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Taxonomic identifieri229533 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

Subcellular locationi

  • Glyoxysome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Isocitrate lyasePRO_0000286157Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi5518.FGSG_09896P0.

Structurei

3D structure databases

ProteinModelPortaliQ4HYR2.
SMRiQ4HYR2. Positions 16-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1083Substrate bindingBy similarity
Regioni216 – 2172Substrate bindingBy similarity
Regioni432 – 4365Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
InParanoidiQ4HYR2.
KOiK01637.
OrthoDBiEOG73Z331.

Family and domain databases

Gene3Di3.20.20.60. 2 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4HYR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQNMTNPS INPDIEDELF QKEVEAVKTW WSDSRWRQTK RPFTAEQIVS
60 70 80 90 100
KRGYLPIDYA SNTQAKKLWK ILEHRFENRD ASYTYGCLEP TMVTQMAKYL
110 120 130 140 150
DTVYVSGWQS SSTASASDEP GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ
160 170 180 190 200
RQERLSVPKE QRANLLNIDY LRPIVADADT GHGGLTAVMK LTKLFIEKGA
210 220 230 240 250
AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA DIMGSDLLAI
260 270 280 290 300
ARTDAEAATL LSTNIDPRDH AFILGSTNST LKPLNDLMIA AEATGKSGAE
310 320 330 340 350
LQRIEDEWLA KANLSSFDDA VAAAIDAGSF SDKAGIKQEY TSRAKGKSNF
360 370 380 390 400
EARAVARQLL GRDIFFDWDA PRTREGYFRL KGGCDCAVNR AIAYAPYCDA
410 420 430 440 450
IWMESKLPDF AQAEQFAQGV HAVWPEKKLA YNLSPSFNWK TAMPRDEQET
460 470 480 490 500
YIRRLAKLGY CWQFITLAGL HTTALISDQF AKAYSTVGMR AYGELVQEPE
510 520 530 540
MDQKVDVVKH QKWSGATYVD ELQKMVTGGI SSTAAMGAGV TEDQFK
Length:546
Mass (Da):60,826
Last modified:August 16, 2005 - v1
Checksum:iC90BD9BFBAB4BE9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231669 Genomic DNA. Translation: ESU16540.1.

Genome annotation databases

KEGGifgr:FG09896.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231669 Genomic DNA. Translation: ESU16540.1.

3D structure databases

ProteinModelPortaliQ4HYR2.
SMRiQ4HYR2. Positions 16-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5518.FGSG_09896P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGifgr:FG09896.1.

Phylogenomic databases

eggNOGiCOG2224.
InParanoidiQ4HYR2.
KOiK01637.
OrthoDBiEOG73Z331.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00719.

Family and domain databases

Gene3Di3.20.20.60. 2 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiACEA_GIBZE
AccessioniPrimary (citable) accession number: Q4HYR2
Secondary accession number(s): V6RX12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: August 16, 2005
Last modified: June 24, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.