ID   ACEA_ACICA              Reviewed;          15 AA.
AC   P28467;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 64.
DE   RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:1938889};
DE            Short=ICL {ECO:0000303|PubMed:1938889};
DE            EC=4.1.3.1 {ECO:0000269|PubMed:1938889};
DE   AltName: Full=Isocitrase {ECO:0000303|PubMed:1938889};
DE   AltName: Full=Isocitratase {ECO:0000303|PubMed:1938889};
DE   Flags: Fragment;
GN   Name=aceA;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC   STRAIN=B4;
RX   PubMed=1938889; DOI=10.1128/jb.173.21.6844-6848.1991;
RA   Hoyt J.C., Johnson K.E., Reeves H.C.;
RT   "Purification and characterization of Acinetobacter calcoaceticus
RT   isocitrate lyase.";
RL   J. Bacteriol. 173:6844-6848(1991).
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:0000269|PubMed:1938889}.
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:0000269|PubMed:1938889};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:1938889};
CC       Note=Divalent metal cations. Mn(2+), Fe(2+) or Co(2+) can be used.
CC       {ECO:0000269|PubMed:1938889};
CC   -!- ACTIVITY REGULATION: Inhibited by hydroxymalonate, oxalate and
CC       itaconate. {ECO:0000269|PubMed:1938889}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for threo-D-isocitrate {ECO:0000269|PubMed:1938889};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:1938889};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000305|PubMed:1938889}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1938889}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   PIR; A41338; A41338.
DR   SABIO-RK; P28467; -.
DR   UniPathway; UPA00703; UER00719.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cobalt; Direct protein sequencing; Glyoxylate bypass; Iron; Lyase;
KW   Magnesium; Manganese; Tricarboxylic acid cycle.
FT   CHAIN           1..>15
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068770"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1710 MW;  83AE726B1F2F96E3 CRC64;
     MTYQTAIDAV RELKA