ID A0A0Q7U621_9MICO Unreviewed; 437 AA.
AC A0A0Q7U621;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ASD19_11705 {ECO:0000313|EMBL:KQZ07891.1};
OS Microbacterium sp. Root53.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQZ07891.1, ECO:0000313|Proteomes:UP000051407};
RN [1] {ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ07891.1, ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|EMBL:KQZ07891.1,
RC ECO:0000313|Proteomes:UP000051407};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ07891.1}.
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DR EMBL; LMFR01000005; KQZ07891.1; -; Genomic_DNA.
DR RefSeq; WP_055988713.1; NZ_LMFR01000005.1.
DR AlphaFoldDB; A0A0Q7U621; -.
DR STRING; 1736553.ASD19_11705; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000051407; 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:KQZ07891.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051407}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 101..103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 322..326
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 437 AA; 47615 MW; 7CF4D51FCD9D9A06 CRC64;
MSTLDQHPMP ARPGDQTQTA DDLRLEWSAD PRWSGIARDY TAEDVIRLRG TVREDATLAR
RGAQTLWQRL ADAEPVRALG AMTGNQAVQQ VRAGLKAIYL SGWQVAADAN LSGQTYPDQS
LYPANSVPAV VRRINNALLR QDQLEHAEGG TTRDWMAPIV ADAEAGFGGP LNAYELAHAM
IQAGAAGIHW EDQLASEKKC GHLGGKVLVP TQQHIRTLNA ARLAADVAGV PTIQIARTDA
LAADLLTSDV DERDRPFLTG GRTSEGFYRV RNGIEPVISR GLAYAPYADL LWVETGTPDV
ELAREFAAAI HAEHPGKMLA YNCSPSFNWR RALSDAEIAS FQDELAALGY RFQFITLAGF
HALNHSMFQL ARGYAENAMT AYVDLQEAEF AAEKDGYTAT KHQREVGTGY FDHVSTALNP
DSATLALVGS TESEQFH
//
