ID B2U6J3_RALPJ Unreviewed; 528 AA.
AC B2U6J3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=Rpic_0542 {ECO:0000313|EMBL:ACD25697.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25697.1};
RN [1] {ECO:0000313|EMBL:ACD25697.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD25697.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD25697.1; -; Genomic_DNA.
DR AlphaFoldDB; B2U6J3; -.
DR STRING; 402626.Rpic_0542; -.
DR KEGG; rpi:Rpic_0542; -.
DR PATRIC; fig|402626.5.peg.1750; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_038243_0_0_4; -.
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:ACD25697.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 528 AA; 58465 MW; B355DB15A9B3AAE6 CRC64;
MAQYQDDIKA VAGLKETHGS AWNAINPEYA ARMRAQNKFK TGLDIAKYTA KIMRADMAAY
DADPSKYTQS LGCWHGFIGQ QKMISIKKHF NSTERRYLYL SGWMVAALRS EFGPLPDQSM
HEKTSVSALI RELYTFLRQA DARELGGLFR ELDAAKDANA KAAIQAKIDN HVTHVVPIIA
DIDAGFGNAE ATYLLAKQFI EAGACCIQIE NQVSDEKQCG HQDGKVTVPH EDFLAKIRAI
RYAFLELGVD DGIIVARTDS LGAGLTKQIA VTNTPGDLGD QYNAFLDCEE LSADQLGNGD
VVIKRDGKLL RPKRLPSNLF QFRAGTGEAR CVLDCITSLQ NGADLLWIET EKPHIAQIGG
MVKEIRKVIP NAKLVYNNSP SFNWTLNFRQ QVYDAMKEAG KDVSAYERGQ LMSTEYDDSE
LAKLADEKIR TFQADASREA GIFHHLITLP TYHTAALSTD NLAKEYFGDQ GMLGYVAGVQ
RKEIRQGIAC VKHQNMSGSD IGDDHKEYFS GEAALKAAGK DNTMNQFH
//
