ACEA_MYCLE
ID ACEA_MYCLE Reviewed; 606 AA.
AC P46831; Q9CBH0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P9WKK7};
DE Short=ICL {ECO:0000250|UniProtKB:P9WKK7};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P9WKK7};
DE AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P9WKK7};
DE AltName: Full=Isocitratase {ECO:0000250|UniProtKB:P9WKK7};
GN Name=aceA; OrderedLocusNames=ML1985;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476188; DOI=10.1111/j.1365-2958.1995.tb02317.x;
RA Fsihi H., Cole S.T.;
RT "The Mycobacterium leprae genome: systematic sequence analysis identifies
RT key catabolic enzymes, ATP-dependent transport systems and a novel polA
RT locus associated with genomic variability.";
RL Mol. Microbiol. 16:909-919(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Involved in the persistence and virulence of Mycobacterium.
CC Catalyzes the reversible formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle during
CC growth on fatty acid substrates. {ECO:0000250|UniProtKB:P9WKK7}.
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:P9WKK7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000250|UniProtKB:P9WKK7}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WKK7}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC30940.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z46257; CAA86357.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC30940.1; ALT_FRAME; Genomic_DNA.
DR PIR; D87157; D87157.
DR PIR; S77654; S77654.
DR AlphaFoldDB; P46831; -.
DR SMR; P46831; -.
DR STRING; 272631.ML1985; -.
DR EnsemblBacteria; CAC30940; CAC30940; CAC30940.
DR KEGG; mle:ML1985; -.
DR Leproma; ML1985; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_019214_1_0_11; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000000806; 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; -; 2.
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 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..606
FT /note="Isocitrate lyase"
FT /id="PRO_0000068778"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 483..487
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 158
FT /note="R -> L (in Ref. 1; CAA86357)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="V -> L (in Ref. 1; CAA86357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 67601 MW; D82CCCADD6B6D384 CRC64;
MAIMDTNTEV HTLFTQEVAA TQQYFDDPRF AGIIRLYTAR QVVEQRGTIP TDYTVARDAA
TAFYARLREL FAAGKSVTTF GPYSPGQAVS LKRMGIEAIY LGGWATSAKG SITEDPGPDL
ASYPLSQVPD DAAVLVRALL AADRNQQYLR LHMTEQQRAA TPAYDYRPFI IADADTGHGG
DSHVRNLIRR FVEIGVPGYH IEDQRPGTKK CGHQGGKVLV PSDEQIKRLN AARFQLDIMR
VPGIIVARTD AEAANLIDSR ADERDQPFLL GATNLKIPSY KACFLALVRC FYELGVKELH
GHLLYALGDG EYAAASAWLD RQGILAQVSG TVNAWQENGK QSIDDLFEQV EYRLLAAWEK
DAGLMTYGEA VEEMLQFGES EGELIGMSPE EWRRFVGRAS LYAAREKAKE LGVDPGWDCE
LAKTPEGYYQ IRGGIQYAIA KSLAAAPFAD ILWMETKTAD LADARQFAEA IHAEFPEQML
AYNLSPSFNW DTTGMSDEEM KRFPEELGKM GFVFNFITYG GHQIDGVAAE EFATALRQDG
MLALARLQRK MRLVESPYRT PQTLVGGPVA MQRWLRPPDV RRQPRPWAKV RPSTSILCRP
RCRRSC
