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Protein

Isocitrate lyase

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in storage lipid mobilization during the growth of higher plant seedling.By similarity

Catalytic activityi

Isocitrate = succinate + glyoxylate.By similarity

Cofactori

Mg2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi175 – 1751MagnesiumBy similarity
Active sitei213 – 2131Proton acceptorBy similarity
Binding sitei250 – 2501SubstrateBy similarity
Binding sitei472 – 4721SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate lyase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

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 lyaseBy similarity (EC:4.1.3.1By similarity)
Short name:
ICLBy similarity
Alternative name(s):
IsocitraseBy similarity
IsocitratsysaseBy similarity
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Subcellular locationi

  1. Glyoxysome By similarity

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 – 576576Isocitrate lyasePRO_0000068802Add
BLAST

Expressioni

Developmental stagei

Expressed maximally during postgerminative growth.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP25248.
SMRiP25248. Positions 9-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1063Substrate bindingBy similarity
Regioni214 – 2152Substrate bindingBy similarity
Regioni437 – 4415Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi574 – 5763Microbody 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.

P25248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASFSVPSM IMEEEGRFEA EVAEVQTWWS SERFKLTRRP YTARDVVALR
60 70 80 90 100
GHLKQGYASN EMAKKLWRTL KSHQANGTAS RTFGALDPVQ VTMMAKHLDT
110 120 130 140 150
IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE
160 170 180 190 200
ARMSMSREER AKTPFVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG
210 220 230 240 250
VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGTETVLVAR
260 270 280 290 300
TDAVAATLIQ SNIDSRDHQF ILGVTNPSLR GKSLSSLLAE GMAVGNNGPA
310 320 330 340 350
LQAIEDQWLS SARLMTFSDA VVEALKRMNL SENEKSRRVN EWLNHARYEN
360 370 380 390 400
CLSNEQGREL AAKLGVTDLF WDWDLPRTRE GFYRFQGSVT AAVVRGWAFA
410 420 430 440 450
QIADLIWMET ASPDLNECTQ FAEGVKSKTP EVMLAYNLSP SFNWDASGMT
460 470 480 490 500
DQQMMEFIPR IARLGYCWQF ITLAGFHADA LVVDTFAKDY ARRGMLAYVE
510 520 530 540 550
RIQREERSNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ
560 570
FKETWTRPGA AGMGEGTSLV VAKSRM
Length:576
Mass (Da):64,326
Last modified:May 1, 1992 - v1
Checksum:i81A87701A4ACC350
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751A → V in CAA73792 (Ref. 3) Curated
Sequence conflicti177 – 1771D → G in CAA73792 (Ref. 3) Curated
Sequence conflicti256 – 2561A → P in CAA73792 (Ref. 3) Curated
Sequence conflicti278 – 2781S → N in CAA73792 (Ref. 3) Curated
Sequence conflicti340 – 3401N → T in CAA73792 (Ref. 3) Curated
Sequence conflicti344 – 3441N → I in CAA73792 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08482 Genomic DNA. Translation: AAA32992.1.
Y13356 mRNA. Translation: CAA73792.1.
PIRiJQ1105. WZRPI.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08482 Genomic DNA. Translation: AAA32992.1.
Y13356 mRNA. Translation: CAA73792.1.
PIRiJQ1105. WZRPI.

3D structure databases

ProteinModelPortaliP25248.
SMRiP25248. Positions 9-535.
ModBaseiSearch...
MobiDBiSearch...

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. "Coordinate expression of transcriptionally regulated isocitrate lyase and malate synthase genes in Brassica napus L."
    Comai L., Dietrich R.A., Maslyar D.J., Baden C.S., Harada J.J.
    Plant Cell 1:293-300(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  2. "Two classes of isocitrate lyase genes are expressed during late embryogeny and postgermination in Brassica napus L."
    Zhang J.Z., Gomez-Pedrozo M., Baden C.S., Harada J.J.
    Mol. Gen. Genet. 238:177-184(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Olesen C., Thomsen K.K., Svendsen I., Brandt A.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Global.
    Tissue: Cotyledon.

Entry informationi

Entry nameiACEA_BRANA
AccessioniPrimary (citable) accession number: P25248
Secondary accession number(s): O04910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 29, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.