ACEA2_MYCTE
ID ACEA2_MYCTE Reviewed; 766 AA.
AC H8F3R6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Isocitrate lyase 2 {ECO:0000303|PubMed:16689789};
DE Short=ICL2 {ECO:0000303|PubMed:16689789};
DE EC=4.1.3.1 {ECO:0000269|PubMed:16689789};
DE AltName: Full=Isocitrase {ECO:0000303|PubMed:16689789};
DE AltName: Full=Isocitratase {ECO:0000303|PubMed:16689789};
DE AltName: Full=Methylisocitrate lyase {ECO:0000303|PubMed:16689789};
DE Short=MICA {ECO:0000303|PubMed:16689789};
DE EC=4.1.3.30 {ECO:0000269|PubMed:16689789};
GN Name=aceAb; OrderedLocusNames=ERDMAN_2108;
OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=652616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22535945; DOI=10.1128/jb.00353-12;
RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL J. Bacteriol. 194:2770-2770(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=16689789; DOI=10.1111/j.1365-2958.2006.05155.x;
RA Munoz-Elias E.J., Upton A.M., Cherian J., McKinney J.D.;
RT "Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism,
RT intracellular growth, and virulence.";
RL Mol. Microbiol. 60:1109-1122(2006).
CC -!- FUNCTION: Involved in the persistence and virulence of M.tuberculosis.
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. It also catalyzes the formation of
CC pyruvate and succinate from 2-methylisocitrate, a key step in the
CC methylcitrate cycle (propionate degradation route).
CC {ECO:0000269|PubMed:16689789}.
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:0000269|PubMed:16689789};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000269|PubMed:16689789};
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:0000305|PubMed:16689789}.
CC -!- DISRUPTION PHENOTYPE: Deletion of icl2 in cells growing on 0.2%
CC propionate shows a slightly decrease of both isocitrate and
CC methylisocitrate lyase activity. {ECO:0000269|PubMed:16689789}.
CC -!- MISCELLANEOUS: Cell growing on 0.2% glucose show barely detectable
CC isocitrate and methylisocitrate lyase activities. On 0.1% and 0.2%
CC propionate, the lyase activities increase more than 10 and 100-fold,
CC respectively. {ECO:0000269|PubMed:16689789}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AP012340; BAL65901.1; -; Genomic_DNA.
DR RefSeq; WP_003409584.1; NZ_KK339487.1.
DR AlphaFoldDB; H8F3R6; -.
DR SMR; H8F3R6; -.
DR EnsemblBacteria; BAL65901; BAL65901; ERDMAN_2108.
DR KEGG; mtn:ERDMAN_2108; -.
DR PATRIC; fig|652616.3.peg.2143; -.
DR HOGENOM; CLU_019214_1_0_11; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000007568; 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:0046421; F:methylisocitrate 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.
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 SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 1: Evidence at protein level;
KW Glyoxylate bypass; Lyase; Magnesium; Metal-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..766
FT /note="Isocitrate lyase 2"
FT /id="PRO_0000432565"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 216..217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 487..491
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 766 AA; 85320 MW; 9F6B78CFAF23B6AA CRC64;
MAIAETDTEV HTPFEQDFEK DVAATQRYFD SSRFAGIIRL YTARQVVEQR GTIPVDHIVA
REAAGAFYER LRELFAARKS ITTFGPYSPG QAVSMKRMGI EAIYLGGWAT SAKGSSTEDP
GPDLASYPLS QVPDDAAVLV RALLTADRNQ HYLRLQMSER QRAATPAYDF RPFIIADADT
GHGGDPHVRN LIRRFVEVGV PGYHIEDQRP GTKKCGHQGG KVLVPSDEQI KRLNAARFQL
DIMRVPGIIV ARTDAEAANL IDSRADERDQ PFLLGATKLD VPSYKSCFLA MVRRFYELGV
KELNGHLLYA LGDSEYAAAG GWLERQGIFG LVSDAVNAWR EDGQQSIDGI FDQVESRFVA
AWEDDAGLMT YGEAVADVLE FGQSEGEPIG MAPEEWRAFA ARASLHAARA KAKELGADPP
WDCELAKTPE GYYQIRGGIP YAIAKSLAAA PFADILWMET KTADLADARQ FAEAIHAEFP
DQMLAYNLSP SFNWDTTGMT DEEMRRFPEE LGKMGFVFNF ITYGGHQIDG VAAEEFATAL
RQDGMLALAR LQRKMRLVES PYRTPQTLVG GPRSDAALAA SSGRTATTKA MGKGSTQHQH
LVQTEVPRKL LEEWLAMWSG HYQLKDKLRV QLRPQRAGSE VLELGIHGES DDKLANVIFQ
PIQDRRGRTI LLVRDQNTFG AELRQKRLMT LIHLWLVHRF KAQAVHYVTP TDDNLYQTSK
MKSHGIFTEV NQEVGEIIVA EVNHPRIAEL LTPDRVALRK LITKEA
