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Database: UniProt
Entry: A0A2B4S464_STYPI
LinkDB: A0A2B4S464_STYPI
Original site: A0A2B4S464_STYPI 
ID   A0A2B4S464_STYPI        Unreviewed;       452 AA.
AC   A0A2B4S464;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE            EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
GN   Name=aceA {ECO:0000313|EMBL:PFX24691.1};
GN   ORFNames=AWC38_SpisGene10695 {ECO:0000313|EMBL:PFX24691.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24691.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
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   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
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:PFX24691.1}.
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DR   EMBL; LSMT01000169; PFX24691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4S464; -.
DR   STRING; 50429.A0A2B4S464; -.
DR   EnsemblMetazoa; XM_022936355.1; XP_022792090.1; LOC111331283.
DR   OrthoDB; 983054at2759; -.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PFX24691.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         99..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         321..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   452 AA;  50056 MW;  CA1216C936200F43 CRC64;
     MQFLRQPLAV NKLNRRLFPR LSTRKKYHIV SALRDYGPEV VEKLRGTIKV EYTLARRGAD
     RLWEMIYRGE GSYVNALGAM TGGQAVQMAK AGLQSIYLSG WQVAADSNMA SQTYPDQSLY
     PVNSAAKLVE RINNAFIRAD QIAHMEGKDH HIDFFLPIVA DCEAGFGGPL NAFEITKSMI
     TAGAAGVHFE DQVASEKKCG HMGGKVLLPT QQFIKVLNAA RLATDVMGVP TVIIGRTDAE
     SAALVTSDID PRDQPFLTGE RTAEGFYRST AGLQQAIARG LSYAPYCDVI WCETGKPNLD
     EAHMFSDAIH SMFPGKPLAY NCSPSFNWKA NLSDKEIAEF QKELGKMGYR YQFITLAGFH
     SLNHAMFKLA RDYRDHGMSA YTKIQEDEFA QAQFGFTAHK HQREVGTGYF DQVSMAISGG
     TSSTTALEGS TETEQFCNKK SVLINEKQSF GR
//
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