ID A0A0Q5LAW6_9BURK Unreviewed; 443 AA.
AC A0A0Q5LAW6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ASF94_08030 {ECO:0000313|EMBL:KQR45722.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR45722.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR45722.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR45722.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR45722.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR45722.1,
RC ECO:0000313|Proteomes:UP000051403};
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:KQR45722.1}.
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DR EMBL; LMOV01000024; KQR45722.1; -; Genomic_DNA.
DR RefSeq; WP_056667382.1; NZ_LMOV01000024.1.
DR AlphaFoldDB; A0A0Q5LAW6; -.
DR STRING; 1736280.ASF94_08030; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000051403; 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:KQR45722.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051403}.
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 325..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 443 AA; 48693 MW; 60F41B15337EB120 CRC64;
MPQSLNAQLS REQQIAALEL DWAQNPRWKG VKRNYSAADV VRLRGSVQPE HTYAQRGAEK
LWDKINGGAK KGYVNAFGAI SAGQAMQQAK AGLEAVYLSG WQVAADGNTS ETMYPDQSLY
AYDSVPTMVR RINNTFKRAD EIQWGRGVNP GDKEFIDYFL PIVADAEAGF GGVLNAFELM
KNMIAAGAAG VHFEDQLAAV KKCGHMGGKV LVPTQEAIEK LLAARFAADT MGVPTIILAR
TDAEAANLIT SDHDANDKPF LTGERTQEGF YRVKNGLEQA ISRGVAYAPY ADLVWCETGV
PDIGFAREFA QAVHAACPGK LLSYNCSPSF NWKKNLNEKQ IASFQEDLSA LGYKYQFITL
AGIHINWYNT FQFAHAYARG EGMKHYTEMV QEPEFAAREK GYTFVSHQQE VGAGYFDDVT
TVIQGGSSSV KALTGSTEEE QFH
//
