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Protein

Isocitrate lyase

Gene

ICL1

Organism
Candida tropicalis (Yeast)
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:iglyoxylate 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, glyoxysomal (PMS1)
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 bindingi172 – 1721MagnesiumBy similarity
Active sitei210 – 2101Proton acceptorBy similarity
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei464 – 4641SubstrateBy 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
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

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 – 550550Isocitrate lyasePRO_0000068786Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi294747.XP_002550404.1.

Structurei

3D structure databases

ProteinModelPortaliP20014.
SMRiP20014. Positions 8-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni101 – 1033Substrate bindingBy similarity
Regioni211 – 2122Substrate bindingBy similarity
Regioni430 – 4345Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi548 – 5503Microbody targeting signalSequence Analysis

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.

P20014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYTKIDINQ EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL
60 70 80 90 100
KIAYPSSQQS DKLFKLLEKH DAEKSVSFTF GALDPIHVAQ MAKYLDSIYV
110 120 130 140 150
SGWQCSSTAS TSNEPSPDLA DYPMDTVPNK VEHLWFAQLF HDRKQREERL
160 170 180 190 200
NMTKEERANT PYIDFLRPII ADADTGHGGI TAIIKLTKLF IERGAAGIHI
210 220 230 240 250
EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS NLLAVARTDS
260 270 280 290 300
EAATLITSTI DHRDHYFIIG ATNPESGDLA ALMAEAEAKG IYGDELARIE
310 320 330 340 350
TEWTKKAGLK LFHEAVIDEI KAGNYSNKEA LIKKFTDKVN PLSHTSHKEA
360 370 380 390 400
KKLAKELTGK DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW
410 420 430 440 450
MESALPDYNQ AKEFADGVKA AVPDQWLAYN LSPSFNWNKA MPADEQETYI
460 470 480 490 500
KRLGQLGYVW QFITLAGLHT TALAVDDFAN QYSQIGMRAY GQTVQQPEIE
510 520 530 540 550
KGVEVVKHQK WSGANYIDGL LRMVSGGVTS TAAMGAGVTE DQFKETKAKV
Length:550
Mass (Da):61,577
Last modified:February 1, 1991 - v1
Checksum:iBA86F18169B5AC0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00703 Genomic DNA. Translation: BAA00611.1.
PIRiJX0105. WZCKI.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00703 Genomic DNA. Translation: BAA00611.1.
PIRiJX0105. WZCKI.

3D structure databases

ProteinModelPortaliP20014.
SMRiP20014. Positions 8-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi294747.XP_002550404.1.

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. "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization."
    Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A.
    J. Biochem. 107:262-266(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiACEA_CANTR
AccessioniPrimary (citable) accession number: P20014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 24, 2015
This is version 87 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.