ID A0A098U461_9BURK Unreviewed; 526 AA.
AC A0A098U461;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN ORFNames=IA69_26210 {ECO:0000313|EMBL:KGF79126.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF79126.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF79126.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF79126.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-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:KGF79126.1}.
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DR EMBL; JPQD01000039; KGF79126.1; -; Genomic_DNA.
DR RefSeq; WP_036238850.1; NZ_JPQD01000039.1.
DR AlphaFoldDB; A0A098U461; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000029701; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KGF79126.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 526 AA; 58410 MW; 82907E2DE2EA055A CRC64;
MSEYQNDIQA IATLKQRYGS GWDAINPESA ARMRAQNRFK TGLDIARYTA AIMRRDMANY
DADPSKYTQS LGCWHGFIGQ QKLISIKKHF NSTDRRYLYL SGWMIAALRS EFGPLPDQSM
HEKTAVPALI KELYTFLRQA DARELGGLFR QLDAAEGAAK AAIQDKIDNF VTHVVPIIAD
IDAGFGNAEA TYLLAKQMIE AGACCIQLEN QVSDEKQCGH QDGKVTVPHE DFLAKIRAVR
YAFLELGVDD GVIVARTDSL GAGLTKQIAV THEPGDLGDQ YNSFLDAEEI AAAELKNGDV
VIQRNGKLLR PKRLASNLFQ FREGTGEARC VLDCITSLQN GADLLWIETE KPHIGQIGGM
VREIRKVIPN AKLVYNNSPS FNWTLNFRQQ VYDGMKDRGE DVSAYDRAHL MSAEYDDSIL
AKVADERIRT FQADAAREAG IFHHLITLPT YHTAALSTDN LAKDYFGNQG MLGYVAGVQR
KEIRQGIACV KHQNMSGSDI GDDHKEYFSG EAALKAGGKH NTMNQF
//