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Database: UniProt
Entry: A0A101P0W6_9ACTN
LinkDB: A0A101P0W6_9ACTN
Original site: A0A101P0W6_9ACTN 
ID   A0A101P0W6_9ACTN        Unreviewed;       427 AA.
AC   A0A101P0W6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AQI95_25480 {ECO:0000313|EMBL:KUN02882.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN02882.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN02882.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN02882.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
RL   Submitted (OCT-2015) 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:KUN02882.1}.
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DR   EMBL; LMWN01000036; KUN02882.1; -; Genomic_DNA.
DR   RefSeq; WP_067128220.1; NZ_KQ948215.1.
DR   AlphaFoldDB; A0A101P0W6; -.
DR   STRING; 67386.AQI95_25480; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000053127; 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; 2.
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:KUN02882.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053127}.
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         90..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         191..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         312..316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   427 AA;  46533 MW;  D3485B759AF67045 CRC64;
     MAETRTQAAE ELARRWATDP RWQGIERTYT AQDVIRLSGS VREEHTLARR GAERLWRQLH
     ERDYVHALGA LTGGQAVQQV KAGLQAIYLS GWQVAADANQ AGHTYPDQSL YPANSVPQVV
     RRINNALLRA DQIATAEDAG DTTDWLAPIV ADAEAGFGGP LNAFELTKAM IAAGAAGIHY
     EDQLASEKKC GHLGGKVLVP TAQHIRTLNA ARLAADIADV PTVVVARTDA LAANLLTSDV
     DERDAEFVTG ERTAEGFYRV RGGMAPVIAR GLAYAPYADL IWVETGTPDL AQAREFAEAV
     HARHPDQMLA YNCSPSFNWK AALDDDQIAK FQRELGAMGY RFQFITLAGF HSLNHGMFDL
     ARGYAEHGMT AYVDLQEREF AAQAHGFTAV RHQREVGTGY FDLVSTAVNP ASSTTALAGS
     TEEEQFH
//
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