ID A0A2U3AQE4_9BACL Unreviewed; 425 AA.
AC A0A2U3AQE4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=DEX24_00230 {ECO:0000313|EMBL:PWI26763.1};
OS Kurthia sibirica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=202750 {ECO:0000313|EMBL:PWI26763.1, ECO:0000313|Proteomes:UP000245938};
RN [1] {ECO:0000313|EMBL:PWI26763.1, ECO:0000313|Proteomes:UP000245938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49154 {ECO:0000313|EMBL:PWI26763.1,
RC ECO:0000313|Proteomes:UP000245938};
RA Maclea K.S., Goen A.E.;
RT "Kurthia sibirica genome sequence.";
RL Submitted (MAY-2018) 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:PWI26763.1}.
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DR EMBL; QFVR01000001; PWI26763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3AQE4; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000245938; 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; 1.
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:PWI26763.1};
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:UP000245938}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 309..313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 425 AA; 46411 MW; 8F3E590B8B6DC5F7 CRC64;
MTVQQIKELQ ENWAQDGRWL GIERPYTAED VLKLRGSVVI EHTLATKGAA RLWQSLHEED
FVNALGALTG NQAMQQVKAG LKAIYLSGWQ VAADANISGQ MYPDQSLYPA NSVPQVVKRI
NQALQRADQI DHAEGRNDDF DWFAPIVADA EAGFGGPLNV FELIKGMIEA GAAGIHLEDQ
LASEKKCGHL GGKVLLPTQN AIRNLVAARL AADVSGVNTI IIARTDADAA DMVTSDIDPR
DADFITGERT PEGFFRTKPG IDQAISRGLA YAPYADLVWC ETSKPDLAEA QKFADAIHAK
FPDKMLAYNC SPSFNWEANL DEETIAKYQV ELGKMGYKFQ FVTLAGFHAL NHSMFQLAND
YRDNGMAAYS KLQQAEFADE AAGYTATKHQ REVGTGYFDE VSQVISGGTS STTAMKGSTE
TAQFI
//
