ID A0A031K327_9SPHN Unreviewed; 528 AA.
AC A0A031K327;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=BV97_00814 {ECO:0000313|EMBL:EZP83629.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP83629.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP83629.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP83629.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) 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:EZP83629.1}.
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DR EMBL; JFYZ01000002; EZP83629.1; -; Genomic_DNA.
DR RefSeq; WP_036523533.1; NZ_JFYZ01000002.1.
DR AlphaFoldDB; A0A031K327; -.
DR STRING; 158500.BES08_08870; -.
DR PATRIC; fig|158500.4.peg.835; -.
DR eggNOG; COG2224; Bacteria.
DR Proteomes; UP000024329; 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; 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:EZP83629.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 528 AA; 58590 MW; 67690AEA56D2DF2E CRC64;
MTYQSKIIEA GNTIGTETHW NGIEAESVAR MRLQNRFQTG LDIARYTAGI MREDMAAYDL
DPANYTQSLG CWHGFIGQQK MISIKKHFGT TKGRYLYLSG WMVAALRSEF GPLPDQSMHE
KTSVPALIEE LYTFLRQADA RELGGMFRDL DKAREGGDEV EAKRIEHAID AYETHVVPIV
ADIDAGFGNA EATYLLAKKF IEAGACCIQI ENQVSDEKQC GHQDGKVTVP HEDFIAKIRA
VRYAFMELGV DEGLIVARTD SLGAGLTKQI AFTRQAGDIG DQYNAFLDCE EVETVGHGDV
LISRDGKLLR PKRLPSNLYQ FRSGTGEDRC VLDSIHALQN GADLLWIETE KPHIGQIGGM
VSRIREVIPN AKLVYNNSPS FNWTLNFRQQ VFDAWQAAGK DVSAFDRARL MSIDYDATEL
AAEADERIRT FQKDAAREAG IFHHLITLPT YHTAALSTDN LAKEYFGDAG MLGYVKGVQR
EEIRQGIACV KHQNMAGSDL GDDHKEYFAG EAALKAGGAH NTMNQFAA
//
