Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Isocitrate lyase

Gene

acu-3

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 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

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771MagnesiumBy similarity
Active sitei215 – 2151Proton acceptorBy similarity
Binding sitei252 – 2521SubstrateBy similarity
Binding sitei468 – 4681SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
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:acu-31 Publication
ORF Names:2E4.10, NCU04230
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 2, Linkage Group V

Subcellular locationi

Glyoxysome 1 Publication

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Isocitrate lyasePRO_0000068794Add
BLAST

Expressioni

Inductioni

By acetate.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi5141.NCU04230.1.

Structurei

3D structure databases

ProteinModelPortaliP28299.
SMRiP28299. Positions 16-531.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1083Substrate bindingBy similarity
Regioni216 – 2172Substrate bindingBy similarity
Regioni434 – 4385Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
InParanoidiP28299.
KOiK01637.
OMAiEMEQGVD.
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.

P28299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANNMVNPA VDPALEDELF AKEVEEVKKW WSDSRWRQTK RPFTAEQIVS
60 70 80 90 100
KRGNLKIEYA SNAQAKKLWK ILEDRFAKRD ASYTYGCLEP TMVTQMAKYL
110 120 130 140 150
DTVYVSGWQS SSTASSSDEP GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ
160 170 180 190 200
RQERLSVPKD QREKLANIDY LRPIVADADT GHGGLTAVMK LTKLFIEKGA
210 220 230 240 250
AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA DIMGSDLLCI
260 270 280 290 300
ARTDAEAATL ITTTIDPRDH AFILGCTNPD LEPLADLMMK AEAEGKTGAQ
310 320 330 340 350
LQAIEDDWLA KADLKRFDEA VLDVIAKGKF SNAKDLAAKY QAAVKGKQIS
360 370 380 390 400
NREARAIARQ LLGQEIFFDW ESPRTREGYY RLKGGCDCSI NRAISYAPYC
410 420 430 440 450
DAIWMESKLP DYAQAEEFAK GVHAVWPEQK LAYNLSPSFN WKTAMGRDDQ
460 470 480 490 500
ETYIRRLAKL GYCWQFITLA GLHTTALISD QFAKAYSKIG MRAYGELVQE
510 520 530 540
PEIDNGVDVV KHQKWSGATY VDELQKMVTG GVSSTAAMGK GVTEDQFH
Length:548
Mass (Da):61,214
Last modified:June 1, 2001 - v2
Checksum:i4C3414CE0794D44C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321V → C in CAA44573 (PubMed:1531185).Curated
Sequence conflicti286 – 2861D → H in CAA44573 (PubMed:1531185).Curated
Sequence conflicti422 – 4243VHA → PR in CAA44573 (PubMed:1531185).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62697 Genomic DNA. Translation: CAA44573.1.
AL451022 Genomic DNA. Translation: CAC18302.1.
CM002240 Genomic DNA. Translation: EAA31618.1.
PIRiS26858.
RefSeqiXP_960854.1. XM_955761.2.
UniGeneiNcr.25128.

Genome annotation databases

EnsemblFungiiEFNCRT00000003928; EFNCRP00000003928; EFNCRG00000003923.
GeneIDi3877001.
KEGGincr:NCU04230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62697 Genomic DNA. Translation: CAA44573.1.
AL451022 Genomic DNA. Translation: CAC18302.1.
CM002240 Genomic DNA. Translation: EAA31618.1.
PIRiS26858.
RefSeqiXP_960854.1. XM_955761.2.
UniGeneiNcr.25128.

3D structure databases

ProteinModelPortaliP28299.
SMRiP28299. Positions 16-531.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU04230.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003928; EFNCRP00000003928; EFNCRG00000003923.
GeneIDi3877001.
KEGGincr:NCU04230.

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
InParanoidiP28299.
KOiK01637.
OMAiEMEQGVD.
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. "Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus nidulans (acuD) and Neurospora crassa (acu-3)."
    Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.
    Curr. Genet. 21:43-47(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: 74A.
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  4. "Particulate enzymes of the glyoxylate cycle in Neurospora crassa."
    Kobr M.J., Vanderhaeghe F., Combepine G.
    Biochem. Biophys. Res. Commun. 37:640-645(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACEA_NEUCR
AccessioniPrimary (citable) accession number: P28299
Secondary accession number(s): Q7RVC2, Q9HEI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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.