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Protein

Isocitrate lyase

Gene

ICL1

Organism
Leptosphaeria maculans (Blackleg fungus) (Phoma lingam)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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). Plays an important role in plant pathogenicity.By similarity1 Publication

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. no protein annotated in this organism
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 bindingi168 – 1681MagnesiumBy similarity
Active sitei206 – 2061Proton acceptorBy similarity
Binding sitei243 – 2431SubstrateBy similarity
Binding sitei457 – 4571SubstrateBy 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 lyase1 Publication (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:ICL11 Publication
OrganismiLeptosphaeria maculans (Blackleg fungus) (Phoma lingam)
Taxonomic identifieri5022 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans complex

Subcellular locationi

  • Glyoxysome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

Pathology & Biotechi

Disruption phenotypei

Leads to limited hyphal growth in plants and extremely low germination rate of pycnidiospores.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 537537Isocitrate lyasePRO_0000068792Add
BLAST

Expressioni

Inductioni

Expression is induced by starvation and acetate.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi5022.CBY01221.

Structurei

3D structure databases

ProteinModelPortaliQ86ZF1.
SMRiQ86ZF1. Positions 2-520.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate bindingBy similarity
Regioni207 – 2082Substrate bindingBy similarity
Regioni423 – 4275Substrate bindingBy similarity

Sequence similaritiesi

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.

Q86ZF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHMDAEDAQ FQKEVAEVKQ WWNDSRWRYT KRTFTAEEIV SKRGNLKITY
60 70 80 90 100
PSNSQSKKLW NIVEHRFKNK DVSYTYGCLD PVMVTQMAKY LDTVYVSGWQ
110 120 130 140 150
ASSTASSTDE PGPDLADYPY TTVPNKVGHL FMAQLFHDRK QREERLTTPK
160 170 180 190 200
ADRAKVANVD YLRPIIADAD TGHGGLTAIM KLTKLFIEKG AAGIHIEDQA
210 220 230 240 250
PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA VARTDSEAAT
260 270 280 290 300
LITSTIDPRD HYYIQGCTNP ALQPLSELMY AAEQSGKSGS ELQAIEDAWV
310 320 330 340 350
KEANLKLFHE AVVDTINAGV HVNKQELINQ FLEQSKGKSN AEARTIAQGL
360 370 380 390 400
TGVDVYFNWD AARTREGYYR YKGGCQCAIN RAIAYAPFCD MIWMESKLPD
410 420 430 440 450
YAQAKEFADG VHAVWPEQKL AYNLSPSFNW KAAMPRDEQE TYIQRLAQLG
460 470 480 490 500
YCWQFITLAG LHQSALMADT FSKAYSKQGM RAYGEIIQEP EAENKVDVLT
510 520 530
HQKWSGANYV DNMLKMVSGG VSSTAAMGKG VTEDQFK
Length:537
Mass (Da):60,126
Last modified:June 1, 2003 - v1
Checksum:i681DDBDD138CAC92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY118108 Genomic DNA. Translation: AAM89498.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY118108 Genomic DNA. Translation: AAM89498.1.

3D structure databases

ProteinModelPortaliQ86ZF1.
SMRiQ86ZF1. Positions 2-520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5022.CBY01221.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Isocitrate lyase is essential for pathogenicity of the fungus Leptosphaeria maculans on canola (Brassica napus)."
    Idnurm A., Howlett B.J.
    Eukaryot. Cell 1:719-724(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE, FUNCTION.

Entry informationi

Entry nameiACEA_LEPMC
AccessioniPrimary (citable) accession number: Q86ZF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 58 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.