ID   ACEA_CORGL              Reviewed;         432 AA.
AC   P42449;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:8206824};
DE            Short=ICL {ECO:0000303|PubMed:8206824};
DE            EC=4.1.3.1 {ECO:0000269|PubMed:8206824};
DE   AltName: Full=Isocitrase {ECO:0000303|PubMed:8206824};
DE   AltName: Full=Isocitratase {ECO:0000303|PubMed:8206824};
GN   Name=aceA {ECO:0000303|PubMed:8206824};
GN   OrderedLocusNames=Cgl2331, cg2560;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE,
RP   ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=8206824; DOI=10.1128/jb.176.12.3474-3483.1994;
RA   Reinscheid D.J., Eikmanns B.J., Sahm H.;
RT   "Characterization of the isocitrate lyase gene from Corynebacterium
RT   glutamicum and biochemical analysis of the enzyme.";
RL   J. Bacteriol. 176:3474-3483(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [4]
RP   INDUCTION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA   Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT   "RamB, a novel transcriptional regulator of genes involved in acetate
RT   metabolism of Corynebacterium glutamicum.";
RL   J. Bacteriol. 186:2798-2809(2004).
RN   [5]
RP   INDUCTION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=16547043; DOI=10.1128/jb.188.7.2554-2567.2006;
RA   Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.;
RT   "Identification of RamA, a novel LuxR-type transcriptional regulator of
RT   genes involved in acetate metabolism of Corynebacterium glutamicum.";
RL   J. Bacteriol. 188:2554-2567(2006).
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:8206824}.
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:8206824};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8206824};
CC       Note=Divalent metal cations. Mn(2+) or Co(2+) can be used.
CC       {ECO:0000269|PubMed:8206824};
CC   -!- ACTIVITY REGULATION: Inhibited by 3-phosphoglycerate, 6-
CC       phosphogluconate, phosphoenolpyruvate (PEP), fructose 1,6-bisphosphate,
CC       glycolate, oxalate, and itaconate. {ECO:0000269|PubMed:8206824}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.28 mM for threo-D-isocitrate {ECO:0000269|PubMed:8206824};
CC         KM=0.34 mM for glyoxylate {ECO:0000269|PubMed:8206824};
CC         KM=0.61 mM for succinate {ECO:0000269|PubMed:8206824};
CC       pH dependence:
CC         Optimum pH is 7.3. {ECO:0000269|PubMed:8206824};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Above 45 degrees Celsius,
CC         the enzyme is denaturated. {ECO:0000269|PubMed:8206824};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000305|PubMed:8206824}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8206824}.
CC   -!- INDUCTION: Activated by RamA and repressed by RamB.
CC       {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:16547043}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       acetate as carbon source. {ECO:0000269|PubMed:8206824}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; X75504; CAA53219.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99724.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20674.1; -; Genomic_DNA.
DR   PIR; I40713; I40713.
DR   RefSeq; NP_601531.1; NC_003450.3.
DR   RefSeq; WP_003859378.1; NC_006958.1.
DR   AlphaFoldDB; P42449; -.
DR   SMR; P42449; -.
DR   DIP; DIP-2898N; -.
DR   STRING; 196627.cg2560; -.
DR   GeneID; 69622606; -.
DR   KEGG; cgb:cg2560; -.
DR   KEGG; cgl:Cgl2331; -.
DR   PATRIC; fig|196627.13.peg.2264; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_11; -.
DR   OrthoDB; 8629576at2; -.
DR   BioCyc; CORYNE:G18NG-11928-MONOMER; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000000582; Chromosome.
DR   Proteomes; UP000001009; 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   1: Evidence at protein level;
KW   Cobalt; Direct protein sequencing; Glyoxylate bypass; Lyase; Magnesium;
KW   Manganese; Metal-binding; Reference proteome; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8206824"
FT   CHAIN           2..432
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000068773"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         93..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         315..319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ   SEQUENCE   432 AA;  47228 MW;  F8B50DA176D32E87 CRC64;
     MSNVGKPRTA QEIQQDWDTN PRWNGITRDY TADQVADLQG SVIEEHTLAR RGSEILWDAV
     TQEGDGYINA LGALTGNQAV QQVRAGLKAV YLSGWQVAGD ANLSGHTYPD QSLYPANSVP
     SVVRRINNAL LRSDEIARTE GDTSVDNWVV PIVADGEAGF GGALNVYELQ KAMIAAGAAG
     THWEDQLASE KKCGHLGGKV LIPTQQHIRT LNSARLAADV ANTPTVVIAR TDAEAATLIT
     SDVDERDQPF ITGERTAEGY YHVKNGLEPC IARAKSYAPY ADMIWMETGT PDLELAKKFA
     EGVRSEFPDQ LLSYNCSPSF NWSAHLEADE IAKFQKELGA MGFKFQFITL AGFHSLNYGM
     FDLAYGYARE GMTSFVDLQN REFKAAEERG FTAVKHQREV GAGYFDQIAT TVDPNSSTTA
     LKGSTEEGQF HN
//