ID   ACEA_RHOFA              Reviewed;         429 AA.
AC   P41554;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:8045408};
DE            Short=ICL {ECO:0000303|PubMed:8045408};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:P0A9G6};
DE   AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P0A9G6};
DE   AltName: Full=Isocitratase {ECO:0000250|UniProtKB:P0A9G6};
GN   Name=icl {ECO:0000303|PubMed:8045408};
OS   Rhodococcus fascians.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=8045408; DOI=10.1016/0378-1119(94)90331-x;
RA   Vereecke D., Villarroel R., van Montagu M., Desomer J.;
RT   "Cloning and sequence analysis of the gene encoding isocitrate lyase from
RT   Rhodococcus fascians.";
RL   Gene 145:109-114(1994).
CC   -!- FUNCTION: Involved in the metabolic adaptation in response to
CC       environmental changes. Catalyzes the reversible formation of succinate
CC       and glyoxylate from isocitrate, a key step of the glyoxylate cycle,
CC       which operates as an anaplerotic route for replenishing the
CC       tricarboxylic acid cycle during growth on fatty acid substrates.
CC       {ECO:0000250|UniProtKB:P0A9G6}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P0A9G6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A9G6};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000250|UniProtKB:P0A9G6}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9G6}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; Z29367; CAA82555.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41554; -.
DR   SMR; P41554; -.
DR   STRING; 1443905.GCA_000761075_05051; -.
DR   eggNOG; COG2224; Bacteria.
DR   UniPathway; UPA00703; UER00719.
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; -; 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   PANTHER; PTHR21631; PTHR21631; 1.
DR   Pfam; PF00463; ICL; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR01346; isocit_lyase; 2.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Lyase; Magnesium; Metal-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..429
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068781"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         91..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         192..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         313..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   429 AA;  46900 MW;  EDBD9D5A2FF6BA0C CRC64;
     MSTTGTPKTT AEIQQDWDTN PRWKGVTRNF TAQQVSDLQG TVVEEATLAR RGSEILWDLV
     NNEDYINSLG ALTGNQAVQQ IRAGLQAIYL SGWQVAGDAN LSGHTYPDQS LYPANSVPSV
     VRRINNALLR ADEIAKIEGD TSVKNWVAPI VADAEAGFGG ALNAYELQKA MIVAGAAGVH
     WEDQLASEKK CGHLGGKVLI PTQQHIRTLT SARLASDVAD VPSVIIARTD AEAATLITSD
     VDERDREFLD GTRTAEGFFG VKNGIEPCIA RAKAYAPYAD LIWMETGVPD LEVAKKFSES
     VRSEFPDQLL AYNWSPSFNW KAHLDDATIA KFQKELGAMG FKFQFITLAG FHSLNYGMFD
     LAHGYAREGM TAFVDLQERE FKAAEERGFT AIKHQREVGA GYFDRIATTV DPNTSTAALK
     GSTEEGQFH