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Database: UniProt
Entry: C3MNS6_SULIL
LinkDB: C3MNS6_SULIL
Original site: C3MNS6_SULIL 
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
//
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