ID A0A2S2CTL8_9PROT Unreviewed; 425 AA.
AC A0A2S2CTL8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
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=DEW08_17505 {ECO:0000313|EMBL:AWK87755.1};
OS Azospirillum thermophilum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK87755.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-2018) 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};
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DR EMBL; CP029353; AWK87755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CTL8; -.
DR KEGG; azz:DEW08_17505; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000245629; Chromosome 2.
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; 1.
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:AWK87755.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000245629}.
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 309..313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 425 AA; 46660 MW; AD78BF367DC9CB36 CRC64;
MALDEKTKAA LRAARYEGIK RDYTMDDVKR LSGSVKIEYT LAEMGAQRLW ELLNTEPYIN
TLGALTGNQA MQAVKAGLKA IYLSGWQVAG DANLAGQMYP DQSLYPANSV PAVVERINNA
FKRADEIHHA EGDDSTYWFA PIVADAEAGF GGPLNAFELM KAMIKAGAAG VHFEDQLASE
KKCGHLGGKV LIPTQQHIRT LNAARMGADV CGTSTLVIAR TDAESAQLIT SDIDERDHPF
IDFDSGRTTE GFYRLKKGMG VDHCIARGLA YAPYSDLLWW ETSKPNLDDA RKFAEAIRKE
FPNKLLAYNC SPSFNWKANL DDDTIAKYQR ELGAMGYKFQ FVTLAGFHSL NYSAFMLAKG
YAERGMAAYS ELQQAEFAAE KLGYTATKHQ REVGTGYFDA VATAVSGGTS STTAYKDSTE
ADQFH
//
