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Database: UniProt
Entry: A0A0D2NMC7_9CHLO
LinkDB: A0A0D2NMC7_9CHLO
Original site: A0A0D2NMC7_9CHLO 
ID   A0A0D2NMC7_9CHLO        Unreviewed;       416 AA.
AC   A0A0D2NMC7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE            EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
GN   ORFNames=MNEG_2180 {ECO:0000313|EMBL:KIZ05781.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ05781.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIZ05781.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ05781.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
CC   -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC       higher plant seedling. {ECO:0000256|ARBA:ARBA00003575}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC       Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000256|ARBA:ARBA00004130}.
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DR   EMBL; KK100457; KIZ05781.1; -; Genomic_DNA.
DR   RefSeq; XP_013904800.1; XM_014049346.1.
DR   AlphaFoldDB; A0A0D2NMC7; -.
DR   STRING; 145388.A0A0D2NMC7; -.
DR   GeneID; 25735058; -.
DR   KEGG; mng:MNEG_2180; -.
DR   OrthoDB; 983054at2759; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR006254; Isocitrate_lyase.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01346; isocit_lyase; 1.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 2.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Glyoxysome {ECO:0000256|ARBA:ARBA00022453};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KIZ05781.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         79..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         179..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         300..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   416 AA;  45224 MW;  5A1FC496D955E9D9 CRC64;
     MASSDANRFE GVKRVFTRQD VLQLRGSIHI EHSLARLGAE RLWKLLNEGG DSYVHALGAL
     TGNQAVQQVA GGLRAIYLSG WQVAADANTA LATYPDQSLY PADSVPKVVE RINNAFQRAD
     QIAHAAGKTD THWFAPIVAD AEAGFGGNLN AYELMRALIK AGAAGVHFED QLASAKKCGH
     LGGKVLVPTK EFVAKLQAAR LAADVCDVPT ILIARTDALG AFLLTSDVDE YDRPFCTGER
     TSEGFYCIKG GIDAAIARGL AYAPYADLLW FETSDPSMEE AKKFAKAIHA KFPGKLLAYN
     CSPSFNWKKK LSDEQIATFQ QDLDKLNYKF QFVTLAGFHA LNFSMFSLAR EYATRGMSAY
     ADLQEAEFAA EKLGYAAVKH QTFVGTGYFD MLAQKVVEEG CSTTALAGST EAEQFH
//
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