ACEA_SALTY
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 03-AUG-2022, entry version 136.
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; Proteobacteria; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P51066; -.
DR PRIDE; P51066; -.
DR EnsemblBacteria; AAL23008; AAL23008; STM4184.
DR GeneID; 1255710; -.
DR KEGG; stm:STM4184; -.
DR PATRIC; fig|99287.12.peg.4396; -.
DR HOGENOM; CLU_019214_2_0_6; -.
DR OMA; LEKDWAE; -.
DR PhylomeDB; P51066; -.
DR BioCyc; SENT99287:STM4184-MON; -.
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; -; 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; 2.
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; 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
