ID C3MNS6_SULIL Unreviewed; 437 AA.
AC C3MNS6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
GN OrderedLocusNames=LS215_1004 {ECO:0000313|EMBL:ACP35039.1};
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572 {ECO:0000313|EMBL:ACP35039.1, ECO:0000313|Proteomes:UP000001747};
RN [1] {ECO:0000313|EMBL:ACP35039.1, ECO:0000313|Proteomes:UP000001747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1 {ECO:0000313|Proteomes:UP000001747};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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};
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DR EMBL; CP001399; ACP35039.1; -; Genomic_DNA.
DR RefSeq; WP_012713407.1; NC_012589.1.
DR AlphaFoldDB; C3MNS6; -.
DR GeneID; 7797508; -.
DR KEGG; sis:LS215_1004; -.
DR HOGENOM; CLU_019214_2_0_2; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 9667at2157; -.
DR Proteomes; UP000001747; 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; 1.
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:ACP35039.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 92..94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 192..193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 313..317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 437 AA; 48933 MW; 128F19272C084096 CRC64;
MNIRDKWSEE EKRLEYEWSE DPRWKGIKRN YKPSDVVKLR GSIRIEYSIA KLASHKLWNL
LNTEPYIATF GALTGSQAVE MAKAGLKAIY VSGWQVAADN NLSNQTYPDL SLYPSNSVPN
LVKRLNNALL RADQISWSEG KHDIDYLLPI VADAEAGFGG PIHAFELTKA LIEAGAAGVH
FEDQLAAEKK CGHLGGKVLI PISAFIRVLN AARLASDVLG VPTILIARTD ALNAKYLSND
VDETDNQFLT GKRTSEGYYE IRGGIEYAIA RGLAYAPYAD LLWFETSKPD LEEARQFAEA
IHTHYPGKLL AYNLSPSFNW KKFMDDSKIS RFMNELGEMG YKFQFITLAG WHLINYHTFK
LARAYRNEGM PAYVRLQESE FQAQAEGYTA VSHQREVGTD YFDLVLTIAS GGEASTTAME
GSTEAEQFVE AKQKVLK
//