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Protein

Mitochondrial 2-methylisocitrate lyase

Gene

ICL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate.1 Publication

Catalytic activityi

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

Pathwayi: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei238 – 2381Curated

GO - Molecular functioni

  • isocitrate lyase activity Source: InterPro
  • methylisocitrate lyase activity Source: SGD

GO - Biological processi

  • propionate catabolic process, 2-methylcitrate cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciYEAST:G3O-34168-MONOMER.
UniPathwayiUPA00946.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial 2-methylisocitrate lyase (EC:4.1.3.30)
Short name:
Methylisocitrate lyase
Gene namesi
Name:ICL2
Ordered Locus Names:YPR006C
ORF Names:LPZ6C, YP9723.06C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR006C.
SGDiS000006210. ICL2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Mitochondrial 2-methylisocitrate lyasePRO_0000068800Add
BLAST

Proteomic databases

PeptideAtlasiQ12031.

Expressioni

Inductioni

Repressed by glucose and induced by ethanol and threonine.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi36183. 10 interactions.
DIPiDIP-4593N.
IntActiQ12031. 1 interaction.
MINTiMINT-505141.

Structurei

3D structure databases

ProteinModelPortaliQ12031.
SMRiQ12031. Positions 44-557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00510000053163.
HOGENOMiHOG000238475.
InParanoidiQ12031.
KOiK01637.
OMAiGANYIDG.
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]
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.

Q12031-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITMINNKTF NRKTTGTLKK LVLSSDKSLR RSFNGASSTK DFVFSESSKV
60 70 80 90 100
EEWWESARFK NISRPYSATD VVKHRGSLPA NTSIYPSSYQ ARKLFNLLEE
110 120 130 140 150
NFKNGTPLHT LGVIDPVQMS QLARCRNIKV AYISGWACSS TLVGSTNEVS
160 170 180 190 200
PDFGDYPYDT VPNQVERIFK AQQLHDRKAF LEASIKGSTP VDYLKPIIAD
210 220 230 240 250
ADMGHGGPTT VMKVAKLFAE KGAAGIHLED QMVGGKRCGH LSGAVLVPTA
260 270 280 290 300
THLMRLISTR FQWDIMGTEN LVIARTDSCN GKLLSSSSDP RDHEFIRGII
310 320 330 340 350
RDNVVPWSEK LIEMEDKKIP NSAIADMEKE WYHENELFTF EEALEKQFTA
360 370 380 390 400
SEFESYKEKK EDLMVNKLGR AYLSLREMKL LAQEVTPLKK IIFDWDAPRT
410 420 430 440 450
KEGYYMFNGC IEAAIRRSLV FAPYSDMIWL ETKTPDLEQA RSFSRKIHKQ
460 470 480 490 500
LPATKLVYNL SPSFNWSAHG FDDKALKSFV WDLAKEGFTL QLVSLAGLHS
510 520 530 540 550
DGVSFWELAN SFQSDGMKAY VEKVQKREKE TNCDIMTHQL WSGAEYVDSL
560 570
MKVVQNGASS QTLSTSGESF TETQF
Length:575
Mass (Da):64,976
Last modified:November 1, 1997 - v1
Checksum:iC29A9A62A02BD291
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95046.1.
Z48951 Genomic DNA. Translation: CAA88784.1.
U31900 Genomic DNA. Translation: AAA97585.1.
BK006949 Genomic DNA. Translation: DAA11433.1.
PIRiS52819.
RefSeqiNP_015331.1. NM_001184103.1.

Genome annotation databases

EnsemblFungiiYPR006C; YPR006C; YPR006C.
GeneIDi856114.
KEGGisce:YPR006C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71255 Genomic DNA. Translation: CAA95046.1.
Z48951 Genomic DNA. Translation: CAA88784.1.
U31900 Genomic DNA. Translation: AAA97585.1.
BK006949 Genomic DNA. Translation: DAA11433.1.
PIRiS52819.
RefSeqiNP_015331.1. NM_001184103.1.

3D structure databases

ProteinModelPortaliQ12031.
SMRiQ12031. Positions 44-557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36183. 10 interactions.
DIPiDIP-4593N.
IntActiQ12031. 1 interaction.
MINTiMINT-505141.

Proteomic databases

PeptideAtlasiQ12031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR006C; YPR006C; YPR006C.
GeneIDi856114.
KEGGisce:YPR006C.

Organism-specific databases

EuPathDBiFungiDB:YPR006C.
SGDiS000006210. ICL2.

Phylogenomic databases

GeneTreeiENSGT00510000053163.
HOGENOMiHOG000238475.
InParanoidiQ12031.
KOiK01637.
OMAiGANYIDG.
OrthoDBiEOG73Z331.

Enzyme and pathway databases

UniPathwayiUPA00946.
BioCyciYEAST:G3O-34168-MONOMER.

Miscellaneous databases

NextBioi981184.
PROiQ12031.

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]
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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in Saccharomyces cerevisiae."
    Heinisch J.J., Valdes E., Alvarez J., Rodicio R.
    Yeast 12:1285-1295(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. "The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism."
    Luttik M.A.H., Koetter P., Salomons F.A., van der Klei I.J., van Dijken J.P., Pronk J.T.
    J. Bacteriol. 182:7007-7013(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiACEB_YEAST
AccessioniPrimary (citable) accession number: Q12031
Secondary accession number(s): D6W417
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1084 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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 one 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.