ID A0A074NM05_9SPHN Unreviewed; 531 AA.
AC A0A074NM05;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN ORFNames=EH32_06850 {ECO:0000313|EMBL:KEO98817.1};
OS Erythrobacter litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO98817.1, ECO:0000313|Proteomes:UP000027866};
RN [1] {ECO:0000313|EMBL:KEO98817.1, ECO:0000313|Proteomes:UP000027866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO98817.1,
RC ECO:0000313|Proteomes:UP000027866};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL Submitted (APR-2014) 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:KEO98817.1}.
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DR EMBL; JMIX01000003; KEO98817.1; -; Genomic_DNA.
DR RefSeq; WP_034901202.1; NZ_JMIX01000003.1.
DR AlphaFoldDB; A0A074NM05; -.
DR KEGG; elq:Ga0102493_112689; -.
DR PATRIC; fig|39960.10.peg.1786; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000027866; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KEO98817.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000027866}.
FT ACT_SITE 220
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 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 378..382
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 531 AA; 59059 MW; 146F7B92E6FAB48E CRC64;
MTYQDTIAHM RNVVSANGSW TGIDPESAAR MVIQNRFRTG LDIAKYTAKI MREDMEAYDA
DPSQYTQSLG CWHGFIGQQK MISIKKHFGS TKRRYLYLSG WMVAALRSEF GPLPDQSMHE
KTSVPSLIGE LYTFLKQADA RELGMMFRAL DEAREAGDEV KAREIQKSVD NYETHVVPII
ADIDAGFGNA EATYLLAKKM IEAGACALQI ENQVSDEKQC GHQDGKVTVP HEDFIAKIRA
CRHAFLELGI DDGIIVARTD SLGAGLTKQI AYSKEPGDLG DQYNSFLDAE EVDPANITNG
QVFISRDGKL MAPKRLPSNL YQFRSGTGVD RVVLDCITSL QNGADLLWIE TEKPHVEQIA
SMVDKIRETV PNAKLVYNNS PSFNWTLNFR QQVFDAWVEA GKDVSAYDRT RLMSVDYDGT
DLAAEADAKI RSFQADAAKR AGIFHHLITL PTYHTAALST DNLAREYFGE EAMLGYVKNV
QRKEIREGIA CVKHQNMAGS DIGDDHKEYF AGEAALKAGG KDNTMNQFEA A
//
