ID L8JV12_9BACT Unreviewed; 430 AA.
AC L8JV12;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
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 ORFNames=C900_02760 {ECO:0000313|EMBL:ELR71419.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR71419.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR71419.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR71419.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR71419.1}.
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DR EMBL; AMZN01000040; ELR71419.1; -; Genomic_DNA.
DR RefSeq; WP_009580064.1; NZ_AMZN01000040.1.
DR AlphaFoldDB; L8JV12; -.
DR STRING; 1237149.C900_02760; -.
DR PATRIC; fig|1237149.3.peg.2515; -.
DR eggNOG; COG2224; Bacteria.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000011135; 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; 1.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 1.
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:ELR71419.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 309..313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 430 AA; 47343 MW; FA52197305DB7E99 CRC64;
MSKADQIEKM YSDWMSNPRW KGITRPYIPE DVLKLRGSIN IEYTLAKMGA EKLWKRLTTQ
PFTAGLGALT GNQAIQEVSA GLEAIYLSGW QVAADANLAG QMYPDQSLYP ADSVPNVVKR
INNALMRRDQ IQSVNGDAEI DWLVPIVADA EAGFGGNLNA FELMKAMIEA GAAGVHFEDQ
LSSAKKCGHL GGKVLVPTQE AINKLVAARL AADVMGTPTI LVARTDAEAA NLITSDVDER
DHKFITGKRT GEGFFHVKNG LEQGIDRGLS YAPYADLLWM ETSNPDLGMA REFAQGIKEK
YPDQMLAYNC SPSFNWAAKL SVNEMEGFRE SLAEMGYKFQ FITLAGFHAL NTSMFELSKA
YKERGMAGYS ELQEREFALQ KEGFTAVKHQ AFVGTQYFDT VQNIVQQGLS STTAMKGSTE
EEQFETAKVG
//
