ACEA_ALKHC
ID ACEA_ALKHC Reviewed; 427 AA.
AC Q9K9H0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=BH2677;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06396.1; -; Genomic_DNA.
DR PIR; E83984; E83984.
DR RefSeq; WP_010898826.1; NC_002570.2.
DR AlphaFoldDB; Q9K9H0; -.
DR SMR; Q9K9H0; -.
DR STRING; 272558.10175298; -.
DR EnsemblBacteria; BAB06396; BAB06396; BAB06396.
DR KEGG; bha:BH2677; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_019214_2_0_9; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 152545at2; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001258; 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; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 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..427
FT /note="Isocitrate lyase"
FT /id="PRO_0000068771"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 310..314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 427 AA; 46783 MW; 0C52D4A9F89E0DFE CRC64;
MSGWQETAEK LEMSWSNDVR WQGVERPYSG EEVVKLRGSL KIEYTLAKTG AEKLWKLLHE
EDYVNALGAM TGGQAIQQVK AGLKAIYLSG WQVAADANLA GHMYPDQSLY PANSVPSVVK
RINQALQRAD QIQHLEGEGE VDYFAPIVAD AEAGFGGQLN VFELMKAMIE AGASGVHFED
QLASEKKCGH LGGKVLIPTQ TAIRNLVSAR LAADVMGVPT ILVARTDADA ADLITSDIDP
ADQRFITGER TPEGFYRTNA GIEQAIARGL AYAPYADLIW CETSKPSLEE AKQFADAIHE
KFPGKLLAYN CSPSFNWEAN LDRATIETFQ QELGKMGYKF QFVTLAGFHA LNHSMFELAY
GYKQRGMGAY SELQQAEFAS EVKGYTATRH QREVGTGYFD QVAQTITGGT SSTTALTGST
EEAQFQK
