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
//