ACEA2_MYCBO
ID ACEA2_MYCBO Reviewed; 766 AA.
AC Q7TZA8; A0A1R3XZQ0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Isocitrate lyase 2 {ECO:0000250|UniProtKB:Q8VJU4};
DE Short=ICL2 {ECO:0000250|UniProtKB:Q8VJU4};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:Q8VJU4};
DE AltName: Full=Isocitrase {ECO:0000250|UniProtKB:Q8VJU4};
DE AltName: Full=Isocitratase {ECO:0000250|UniProtKB:Q8VJU4};
GN Name=aceA; OrderedLocusNames=BQ2027_MB1950;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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:Q8VJU4}.
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:Q8VJU4};
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:Q8VJU4}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; LT708304; SIU00553.1; -; Genomic_DNA.
DR RefSeq; NP_855601.1; NC_002945.3.
DR RefSeq; WP_003409584.1; NC_002945.4.
DR AlphaFoldDB; Q7TZA8; -.
DR SMR; Q7TZA8; -.
DR EnsemblBacteria; SIU00553; SIU00553; BQ2027_MB1950.
DR PATRIC; fig|233413.5.peg.2139; -.
DR OMA; WLIHRFK; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001419; 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; -; 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 3: Inferred from homology;
KW Glyoxylate bypass; Lyase; Magnesium; Metal-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..766
FT /note="Isocitrate lyase 2"
FT /id="PRO_0000432563"
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
