ID A0A022QAZ4_ERYGU Unreviewed; 576 AA.
AC A0A022QAZ4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00012909, ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=MIMGU_mgv1a003576mg {ECO:0000313|EMBL:EYU24789.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU24789.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU24789.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(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}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|PIRNR:PIRNR001362}.
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; KI632106; EYU24789.1; -; Genomic_DNA.
DR RefSeq; XP_012852495.1; XM_012997041.1.
DR AlphaFoldDB; A0A022QAZ4; -.
DR STRING; 4155.A0A022QAZ4; -.
DR GeneID; 105972101; -.
DR KEGG; egt:105972101; -.
DR eggNOG; KOG1260; Eukaryota.
DR OMA; YVSGWQV; -.
DR OrthoDB; 983054at2759; -.
DR PhylomeDB; A0A022QAZ4; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0009514; C:glyoxysome; IBA:GO_Central.
DR GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
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; 1.10.10.850; -; 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; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Glyoxysome {ECO:0000256|ARBA:ARBA00022453};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001362};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 437..441
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 576 AA; 64224 MW; 2F68B58086008DAF CRC64;
MSASFSVPSM IMEEEGRFEA EVANVQAWWN TERFKLTRRP YSARDVVSLR GNLPQSYGSN
ELAKKLWRTL KTHQANGTAS RTFGSLDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP
DLADYPYDTV PNKVEHLYMA QQYHDRKQRE ARMSMSREER ARTPFVDYLK PIIADGDTGF
GGATATLKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDI
MGVETVLVAR TDAVAATLIQ TNIDARDHQF ILGATNPALR GKGLAAVLSE AMAAGKTGPE
LQAIEDNWLA MARLKTFSEC VVDAIKGMNI GESEKQRKLS EWMSHSSYDK CLSNENGREI
ADRLGLANLF WDWDLPRTRE GFYRFQGSVN AAIVRGWAFA PHTDIIWMET SSPDIIECTD
FARGVKSTQP ETMLAYNLSP SFNWDASGMS DQQMMDFIPR IAKLGYCWQF ITLAGFHADA
LIIDTFAKDF ARRGMLAYVE KIQREERSHG VDTLAHQKWS GANYYDRVLR TVQGGITSTA
AMGKGVTEEQ FQVTWTREGA TDVGSEGNVV IAKSRM
//
