GCP_CAEEL
ID GCP_CAEEL Reviewed; 968 AA.
AC Q10663; O17353; Q8IA71;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Bifunctional glyoxylate cycle protein;
DE AltName: Full=Gex-3-interacting protein 7;
DE Includes:
DE RecName: Full=Isocitrate lyase;
DE Short=ICL;
DE Short=Isocitrase;
DE Short=Isocitratase;
DE EC=4.1.3.1;
DE Includes:
DE RecName: Full=Malate synthase;
DE EC=2.3.3.9;
GN Name=icl-1; Synonyms=gei-7; ORFNames=C05E4.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), DEVELOPMENTAL STAGE, AND PROTEIN
RP SEQUENCE OF 429-461.
RC STRAIN=Bristol N2;
RX PubMed=7781887; DOI=10.1006/dbio.1995.1156;
RA Liu F., Thatcher J.D., Barral J.M., Epstein H.F.;
RT "Bifunctional glyoxylate cycle protein of Caenorhabditis elegans: a
RT developmentally regulated protein of intestine and muscle.";
RL Dev. Biol. 169:399-414(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=21884719; DOI=10.1016/j.mad.2011.08.004;
RA Gallo M., Park D., Riddle D.L.;
RT "Increased longevity of some C. elegans mitochondrial mutants explained by
RT activation of an alternative energy-producing pathway.";
RL Mech. Ageing Dev. 132:515-518(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10119};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9;
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2.
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q10663-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10663-2; Sequence=VSP_056035, VSP_056036;
CC -!- TISSUE SPECIFICITY: Intestinal and body wall muscle cells.
CC -!- DEVELOPMENTAL STAGE: First detected early in the generation of the
CC clonal E cell lineage that is committed to intestinal development and
CC then increases to maximal levels in actively differentiating intestinal
CC and body wall muscle cells. Highest activity in embryos and falls
CC dramatically during L1 larval development (PubMed:7781887). Expression
CC is highest in L3 larval stage with low levels at other stages
CC (PubMed:21884719). {ECO:0000269|PubMed:21884719,
CC ECO:0000269|PubMed:7781887}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the isocitrate
CC lyase/PEP mutase superfamily. Isocitrate lyase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the malate synthase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85857.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23159; AAA85857.1; ALT_SEQ; mRNA.
DR EMBL; FO080368; CCD63238.1; -; Genomic_DNA.
DR EMBL; FO080368; CCD63239.1; -; Genomic_DNA.
DR PIR; E88940; E88940.
DR RefSeq; NP_001021367.1; NM_001026196.4. [Q10663-2]
DR RefSeq; NP_503306.1; NM_070905.5. [Q10663-1]
DR AlphaFoldDB; Q10663; -.
DR SMR; Q10663; -.
DR BioGRID; 43657; 16.
DR DIP; DIP-25113N; -.
DR STRING; 6239.C05E4.9a; -.
DR iPTMnet; Q10663; -.
DR EPD; Q10663; -.
DR PaxDb; Q10663; -.
DR PeptideAtlas; Q10663; -.
DR PRIDE; Q10663; -.
DR EnsemblMetazoa; C05E4.9a.1; C05E4.9a.1; WBGene00001564. [Q10663-1]
DR EnsemblMetazoa; C05E4.9b.1; C05E4.9b.1; WBGene00001564. [Q10663-2]
DR GeneID; 178583; -.
DR KEGG; cel:CELE_C05E4.9; -.
DR UCSC; C05E4.9a; c. elegans.
DR CTD; 178583; -.
DR WormBase; C05E4.9a; CE23521; WBGene00001564; icl-1. [Q10663-1]
DR WormBase; C05E4.9b; CE32565; WBGene00001564; icl-1. [Q10663-2]
DR eggNOG; KOG1260; Eukaryota.
DR eggNOG; KOG1261; Eukaryota.
DR GeneTree; ENSGT00940000174673; -.
DR HOGENOM; CLU_012853_0_0_1; -.
DR InParanoid; Q10663; -.
DR OMA; IWMETSH; -.
DR OrthoDB; 358540at2759; -.
DR PhylomeDB; Q10663; -.
DR UniPathway; UPA00703; UER00719.
DR UniPathway; UPA00703; UER00720.
DR PRO; PR:Q10663; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001564; Expressed in larva and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0004451; F:isocitrate lyase activity; ISS:WormBase.
DR GO; GO:0004474; F:malate synthase activity; ISS:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0006097; P:glyoxylate cycle; ISS:WormBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR CDD; cd00727; malate_synt_A; 1.
DR Gene3D; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR019830; Malate_synthase_CS.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR TIGRFAMs; TIGR01344; malate_syn_A; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
DR PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glyoxylate bypass; Lyase;
KW Multifunctional enzyme; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..968
FT /note="Bifunctional glyoxylate cycle protein"
FT /id="PRO_0000166874"
FT REGION 1..443
FT /note="Isocitrate lyase"
FT REGION 444..968
FT /note="Malate synthase"
FT ACT_SITE 601
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10119"
FT ACT_SITE 881
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10119"
FT VAR_SEQ 862..863
FT /note="YL -> EP (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_056035"
FT VAR_SEQ 864..968
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_056036"
FT CONFLICT 152
FT /note="D -> H (in Ref. 1; AAA85857)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="A -> R (in Ref. 1; AAA85857)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="R -> A (in Ref. 1; AAA85857)"
FT /evidence="ECO:0000305"
FT CONFLICT 957..968
FT /note="TDAYDRLVSEGY -> DRRLRQACL (in Ref. 1; AAA85857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 108629 MW; 7BAAF979C1F6D31F CRC64;
MSSAAKNFYQ VVKSAPKGRF KGIKRDYTVE DVLKLRGSID IDYTLATRGA NKLWQLLHTE
PFVPALGAQT GNQAVQMVRA GLKAIYLSGW QVAADANSAG DMYPDQSLYP ANSGPELAKR
INRSLRRADQ IEACEAEDYL AQRDWYAPIV ADAEAGFGGA LNCFELMKAY IEAGAAGVHY
EDQLGSEKKC GHMGGKVLIP TAQHIRHLNA SRLAADVCGV PTIIVARTDA ESSRLLTSDI
DPRDHPYIDY EAGRTIEGFY RLKDSTAIQY CIDRAIQYAP YTDLIWMETS HPTIADAREF
AEGVHKQYPD KMFAYNCSPS FNWKKHLSPS QMEKFQKELG AMGFKYQFIT LAGYHANSYS
MFDLARNYKE KGMLAYSGLQ EGEFAAEKHG YTAVKHQREV GTGYFDAVSR AVTGGLSSTT
ALSGSTEEAQ FQTAVASQDE EILSLTAQNV AGDEKILTPD ALRFLHDLNT EFNPRRLRLL
SKRNQVQADI NNSLWFPDFN KETEVLRSDQ GWKGAEIPRD LQDRRVEITG PTDRKMVINA
MNSGANVFMA DFEDSNSPTW RNQLEGQINL YDAVRNNISY THPTTKKEYT LNEKHAVLKV
RPRGWHLPEK HVLIHNQPTS GSLFDFGLFV FHNAKALIAQ GSGPYFYLPK LQSAEEAQLW
ADVFKYTEDK LGLARGTIKC TVLIEHLLAS FQLHEIIHAL KDNIVGLNCG RWDYIFSYIK
TFQNHRKFLL PDRFQIGMTA PFMRNYSLEV IKACHLRGIH AMGGMAAQIP IKHDQVANDK
AFALVRADKE REATDGHDGT WVAHPGLVPL AKRVFDQMMP KPNQISKNLT RANCTKEDLT
VIPEGTRTEA GFRHNISVTL GYLDSWLRGT GCVPLYNLME DAATAEISRA QLWQWLHHDA
KLEDGRTIDA GLVKQTIAAE TERRLIRAGS VVNRIPEAAD LLEKFVTEEK MSDFLTTDAY
DRLVSEGY
