ID   ACEA_ECOL6              Reviewed;         434 AA.
AC   P0A9G7; P05313;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P0A9G6};
DE            Short=ICL {ECO:0000250|UniProtKB:P0A9G6};
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=aceA; OrderedLocusNames=c4972;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P0A9G6}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83398.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83398.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000857856.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0A9G7; -.
DR   SMR; P0A9G7; -.
DR   STRING; 199310.c4972; -.
DR   GeneID; 75204155; -.
DR   KEGG; ecc:c4972; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000001410; Chromosome.
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; 2.
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   3: Inferred from homology;
KW   Glyoxylate bypass; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..434
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068775"
FT   ACT_SITE        195
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         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT   BINDING         317..321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   434 AA;  47522 MW;  F66449CCD1E168E9 CRC64;
     MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA AKMWRLLHGE
     SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN LAASMYPDQS LYPANSVPAV
     VERINNTFRR ADQIQWSAGI EPGDPRYVDY FLPIVADAEA GFGGVLNAFE LMKAMIEAGA
     AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL
     ITSDCDPYDS EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
     FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI TLAGIHSMWF
     NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGTS
     SVTALTGSTE ESQF
//