ID A0A023DE35_9BACI Unreviewed; 428 AA.
AC A0A023DE35;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN Name=aceA {ECO:0000313|EMBL:GAJ39554.1};
GN ORFNames=GCA01S_022_00330 {ECO:0000313|EMBL:GAJ39554.1};
OS Parageobacillus caldoxylosilyticus NBRC 107762.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ39554.1, ECO:0000313|Proteomes:UP000023561};
RN [1] {ECO:0000313|EMBL:GAJ39554.1, ECO:0000313|Proteomes:UP000023561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ39554.1,
RC ECO:0000313|Proteomes:UP000023561};
RA Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S.,
RA Ichikawa N., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC
RT 107762.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023531};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAJ39554.1}.
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DR EMBL; BAWO01000022; GAJ39554.1; -; Genomic_DNA.
DR RefSeq; WP_042408640.1; NZ_BAWO01000022.1.
DR AlphaFoldDB; A0A023DE35; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000023561; Unassembled WGS sequence.
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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 NCBIfam; TIGR01346; isocit_lyase; 2.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 2.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:GAJ39554.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000023561}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 310..314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 428 AA; 47419 MW; B5BDFD98F33A91B0 CRC64;
MASFTERVKQ LEESWKNEER WKGIVRPYSA EDVIKLRGSI DIEYTLARRG AEKLWKLLNS
EDYINALGAL TGNQAVQQVK AGLKAIYLSG WQVAADANLA GQMYPDQSLY PANSVPHVVK
RINQALQRAD QIQYLEGSGD IDYFVPIVAD AEAGFGGQLN VFELMKAMIE AGAAGVHFED
QLSSEKKCGH LGGKVLLPTQ TAVRNLIAAR LAADVMGVPT VLIARTDANA ANLITSDIDP
YDQEFITGER TTEGFYRTRA GLDQAIARGL AYAPYADLIW CETSEPNLEE ARRFAEAIHE
KFPGKLLAYN CSPSFNWKKK LDDETIANFQ KELAKMGYKF QFVTLAGFHT LNYSMFELAR
GYKERGMAAY AELQQAEFAA EKYGYTATKH QREVGTGYFD EVAQVISGGQ SSTIALKGST
EEEQFTTA
//
