ID A0A1I3ND90_9BURK Unreviewed; 434 AA.
AC A0A1I3ND90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
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=SAMN05192543_105337 {ECO:0000313|EMBL:SFJ07293.1};
OS Paraburkholderia megapolitana.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=420953 {ECO:0000313|EMBL:SFJ07293.1, ECO:0000313|Proteomes:UP000199548};
RN [1] {ECO:0000313|EMBL:SFJ07293.1, ECO:0000313|Proteomes:UP000199548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23650 {ECO:0000313|EMBL:SFJ07293.1,
RC ECO:0000313|Proteomes:UP000199548};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOQU01000005; SFJ07293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3ND90; -.
DR STRING; 420953.SAMN05192543_105337; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000199548; 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:SFJ07293.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000199548}.
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 193..194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 314..318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 434 AA; 47827 MW; D875A77E31E1443A CRC64;
MSRQEQAKQL QQQWDTDPRW KGIKRTYTAE DVVRLRGSVP VEHTLAKRGA EKLWELVNTE
PFVNSLGALT GNQAMQQVKA GLKAIYLSGW QVAGDANVAG EMYPDQSLYP ANSVPLVVKR
INNTLTRADQ IQWSEGKNPG DEGYVDFFAP IVADAEAGFG GVLNAFELMK AMIESGASGV
HFEDQLASVK KCGHMGGKVL VPTRENVAKL TAARLAADVS GTPTVLLART DAEAADLVTS
DIDDNDKPFL TGERTVEGFY RTRPGLEQAI SRGLAYAPYA DMIWCETGKP DLEFAKKFAD
AIHKQFPDKL LSYNCSPSFN WKKNLDDATI AKFQKELGAM GYKFQFITLA GFHALNYSMF
NLAHGYARNQ MTAFVEMQQA EFAAAEKGFT AVKHQREVGT GYFDAVTQTV ERDASTTALH
GSTEDEQFFD KKVA
//
