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
//