GenomeNet

Database: UniProt
Entry: B0KMX4_PSEPG
LinkDB: B0KMX4_PSEPG
Original site: B0KMX4_PSEPG 
ID   B0KMX4_PSEPG            Unreviewed;       441 AA.
AC   B0KMX4;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
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   OrderedLocusNames=PputGB1_3687 {ECO:0000313|EMBL:ABY99578.1};
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY99578.1, ECO:0000313|Proteomes:UP000002157};
RN   [1] {ECO:0000313|EMBL:ABY99578.1, ECO:0000313|Proteomes:UP000002157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1 {ECO:0000313|EMBL:ABY99578.1,
RC   ECO:0000313|Proteomes:UP000002157};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000926; ABY99578.1; -; Genomic_DNA.
DR   RefSeq; WP_012273289.1; NC_010322.1.
DR   AlphaFoldDB; B0KMX4; -.
DR   GeneID; 45523173; -.
DR   KEGG; ppg:PputGB1_3687; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   OMA; LEKDWAE; -.
DR   Proteomes; UP000002157; Chromosome.
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:ABY99578.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
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   441 AA;  48687 MW;  3AE1784D2DF92A26 CRC64;
     MALTREQQIA ALEKDWAENP RWKGVTRTYT AADVVRLRGS LQPEHTLARQ GAEKLWKLVT
     QGAHPSFRPE KDFVNCMGAL TGGQAVQQVK AGIQAIYLSG WQVAADNNSA ESMYPDQSLY
     PVDSVPTVVK RINNSFRRAD QIQWKAGKNP GDEGYIDYFA PIVADAEAGF GGVLNAYELM
     KNMIEAGAAG VHFEDQLASV KKCGHMGGKV LVPTQEAVQK LVAARLAADV SGVPTIILAR
     TDANAADLLT SDCDPYDQPF VIGERTREGF YKVRAGLDQA ISRGLAYAPY ADLIWCETAK
     PDLDEARRFA EAIKKEYPDQ ILSYNCSPSF NWKKNLDDAT IAKFQRELSA MGYKHQFITL
     AGIHNMWHGM FNLAHDYARN DMTAYVKLQE QEFADASKGY TFVAHQQEVG TGYFDDMTTV
     IQGGASSVTA LTGSTEEEQF H
//
DBGET integrated database retrieval system