ID   ACEA_SALTY              Reviewed;         434 AA.
AC   P51066;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   27-MAR-2024, entry version 143.
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=STM4184;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-434.
RC   STRAIN=S2978, S2979, S2980, S2983, S2985, S2993, S2995, S3013, S3014,
RC   S3015, S3027, S3041, S3044, S3057, S3333, and S4194;
RX   PubMed=9409817; DOI=10.1093/genetics/147.4.1509;
RA   Nelson K., Wang F.S., Boyd E.F., Selander R.K.;
RT   "Size and sequence polymorphism in the isocitrate dehydrogenase
RT   kinase/phosphatase gene (aceK) and flanking regions in Salmonella enterica
RT   and Escherichia coli.";
RL   Genetics 147:1509-1520(1997).
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; AE006468; AAL23008.1; -; Genomic_DNA.
DR   EMBL; U43344; AAC43867.1; -; Genomic_DNA.
DR   EMBL; U43345; AAC43869.1; -; Genomic_DNA.
DR   EMBL; U43346; AAC43871.1; -; Genomic_DNA.
DR   EMBL; U43347; AAC43872.1; -; Genomic_DNA.
DR   EMBL; U43348; AAC43874.1; -; Genomic_DNA.
DR   EMBL; U43349; AAC43876.1; -; Genomic_DNA.
DR   EMBL; U43350; AAC43878.1; -; Genomic_DNA.
DR   EMBL; U43351; AAC43880.1; -; Genomic_DNA.
DR   EMBL; U43352; AAC43882.1; -; Genomic_DNA.
DR   EMBL; U43353; AAC43884.1; -; Genomic_DNA.
DR   EMBL; U43354; AAC43886.1; -; Genomic_DNA.
DR   EMBL; U43355; AAC43888.1; -; Genomic_DNA.
DR   EMBL; U43356; AAC43890.1; -; Genomic_DNA.
DR   EMBL; U43357; AAC43892.1; -; Genomic_DNA.
DR   EMBL; U43358; AAC43894.1; -; Genomic_DNA.
DR   EMBL; U43359; AAC43896.1; -; Genomic_DNA.
DR   RefSeq; NP_463049.1; NC_003197.2.
DR   RefSeq; WP_000857881.1; NC_003197.2.
DR   AlphaFoldDB; P51066; -.
DR   SMR; P51066; -.
DR   STRING; 99287.STM4184; -.
DR   PaxDb; 99287-STM4184; -.
DR   GeneID; 1255710; -.
DR   KEGG; stm:STM4184; -.
DR   PATRIC; fig|99287.12.peg.4396; -.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   OMA; YVSGWQV; -.
DR   PhylomeDB; P51066; -.
DR   BioCyc; SENT99287:STM4184-MONOMER; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000001014; Chromosome.
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; 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_0000068776"
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"
FT   VARIANT         390
FT                   /note="A -> G (in strain: S3041)"
FT   VARIANT         392
FT                   /note="D -> E (in strain: S3013, S3014, S3015, S3027 and
FT                   S3041)"
FT   VARIANT         432
FT                   /note="A -> S (in strain: S2978, S2979, S2980, S2983,
FT                   S2985, S2993, S2995, S3013, S3014, S3015, S3027, S3041,
FT                   S3044, S3057 and S3333)"
SQ   SEQUENCE   434 AA;  47563 MW;  4ADC46FB4A4A5C60 CRC64;
     MKTRTQQIEE LQKEWTQPRW EGITRPYSAE EVVKLRGSVN PECTLAQLGA AKMWRLLHGE
     AKKGYINSLG ALTGGQALQQ AKAGIEAIYL SGWQVAADAN LASSMYPDQS LYPANSVPAV
     VDRINNTFRR ADQIQWASGI EPNDPRYVDY FLPIVADAEA GFGGVLNAFE LMKSMIEAGA
     AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVMGVPTLVI ARTDADAADL
     ITSDCDPYDS GFITGERTSE GFYRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
     FADAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKYQFI TLAGIHSMWF
     NMFDLAHAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGAS
     SVTALTGSTE EAQF
//