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Database: UniProt
Entry: A0A0D6MUR6_ACEAC
LinkDB: A0A0D6MUR6_ACEAC
Original site: A0A0D6MUR6_ACEAC 
ID   A0A0D6MUR6_ACEAC        Unreviewed;       426 AA.
AC   A0A0D6MUR6; A0A7G1M598;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=Abac_014_019 {ECO:0000313|EMBL:GAN57093.1};
OS   Acetobacter aceti NBRC 14818.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX   NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN57093.1, ECO:0000313|Proteomes:UP000032677};
RN   [1] {ECO:0000313|EMBL:GAN57093.1, ECO:0000313|Proteomes:UP000032677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN57093.1,
RC   ECO:0000313|Proteomes:UP000032677};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL   Submitted (NOV-2012) 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:GAN57093.1}.
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DR   EMBL; BAMU01000014; GAN57093.1; -; Genomic_DNA.
DR   RefSeq; WP_010665993.1; NZ_SLZP01000006.1.
DR   AlphaFoldDB; A0A0D6MUR6; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000032677; 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; 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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:GAN57093.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        184
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         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         185..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         308..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   426 AA;  47003 MW;  03D2EBF83FDFEB31 CRC64;
     MSVEAIEKFI SDKTRFAGIE RDYTAQDVAK LSGSFTVEHT IARMGAERLW KLLHEEPYIN
     SLGALTGNQA MQQVKAGLKA IYLSGWQVAA DANLAGQMYP DQSLYPANSV PNVVSRINNA
     LRRCDEIATL EGKGDKTYWM APIVADAEAG FGGALNVFEL MRSMIAAGAA GVHFEDQLAS
     EKKCGHLGGK VLIPISQHLR SLNSARLAAD VERTPTLLVC RTDAHSAQLL TSDVDERDRP
     FLTGERTAEG FFRIKEGLGV EYAIARCEAY APYADLLWWE TSEPNLKEAE QFAEAIHKKF
     PGKLLAYNCS PSFNWKKKLS EKEIAEYQKT IGKMGYKYQF VTLAGFHALN FSMFQLAKGY
     AERGMAAYSE LQQAEFAAEP EGYTATRHQR EVGTGWFDAV ATTASGGQSS TTAMHGSTEH
     DQFNHH
//
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