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Database: UniProt
Entry: W7WPH6_9BURK
LinkDB: W7WPH6_9BURK
Original site: W7WPH6_9BURK 
ID   W7WPH6_9BURK            Unreviewed;       438 AA.
AC   W7WPH6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   Name=aceA {ECO:0000313|EMBL:EWS61879.1};
GN   ORFNames=Y694_00392 {ECO:0000313|EMBL:EWS61879.1};
OS   Methylibium sp. T29-B.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=1437443 {ECO:0000313|EMBL:EWS61879.1, ECO:0000313|Proteomes:UP000019360};
RN   [1] {ECO:0000313|EMBL:EWS61879.1, ECO:0000313|Proteomes:UP000019360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T29-B {ECO:0000313|EMBL:EWS61879.1,
RC   ECO:0000313|Proteomes:UP000019360};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of the loss-of-function mutant Methylibium sp. T29-B.";
RL   Submitted (DEC-2013) 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:EWS61879.1}.
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DR   EMBL; AZSN01000005; EWS61879.1; -; Genomic_DNA.
DR   RefSeq; WP_011829484.1; NZ_AZSN01000005.1.
DR   AlphaFoldDB; W7WPH6; -.
DR   PATRIC; fig|1437443.4.peg.384; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000019360; 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:EWS61879.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         94..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         320..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   438 AA;  48159 MW;  1D3CACFEB6CC2045 CRC64;
     MSQPTREQQI AALEKDWAEN PRWKGLKRGY SAADVVRLRG SLQPEYTIAK RGAEKLWAQC
     NGASKKGYVN AFGAITAGQA MQQAKAGVEA VYLSGWQVAA DGNTSETMYP DQSLYAYDSV
     PTMVRRINNT FKRADEIQWS RGTGPGDKDF IDYFLPIVAD AEAGFGGVLN AFELMKNMIA
     AGAAGVHFED QLAAVKKCGH MGGKVLVPTQ EACEKLIAAR FAADVMGVST IVLARTDAEA
     ANLITSDHDA NDKPFLTGER TQEGFYRVKN GLEQAISRGV AYAAYADLVW CETGTPDLGF
     AREFAQAVHA KHPGKLLSYN CSPSFNWKKN LDDKTIAVFQ EKLSELGYKY QFITLAGIHI
     NWYNTFQFAQ AYAKGEGMKH YVEMVQEPEF KAREQGYTFV SHQQEVGAGY FDDVTTVIQG
     GSSSVKALTG STEEEQFH
//
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