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Database: UniProt
Entry: A0A0A5GLH6_9BACI
LinkDB: A0A0A5GLH6_9BACI
Original site: A0A0A5GLH6_9BACI 
ID   A0A0A5GLH6_9BACI        Unreviewed;       429 AA.
AC   A0A0A5GLH6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=N781_13275 {ECO:0000313|EMBL:KGX92859.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX92859.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX92859.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX92859.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX92859.1}.
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DR   EMBL; AVPE01000004; KGX92859.1; -; Genomic_DNA.
DR   RefSeq; WP_026799928.1; NZ_AVPE01000004.1.
DR   AlphaFoldDB; A0A0A5GLH6; -.
DR   STRING; 1385510.GCA_000425205_01487; -.
DR   eggNOG; COG2224; Bacteria.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000030528; 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:KGX92859.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030528}.
FT   REGION          407..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         86..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         307..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   429 AA;  47389 MW;  3A7137C779EC53F9 CRC64;
     MNQNRIEQIS ESFEGPRWNG VTRPYTAADV DKLKGSIDIE HTLAKRGAEK LWKLINEEDY
     IHALGALTGN QAMQQVKAGL KAIYLSGWQV AADANLSGQM YPDQSLYPAN SVPHVVKRIN
     QTLQRADQID HMEGNDGTDW FAPIVADAEA GFGGQLNVFE LMKQMIEAGA AGVHFEDQLS
     SEKKCGHLGG KVLLPTQHAV KNLISARLAA DTMGVPTVII ARTDANAANL ITSDVDPYDT
     PFMTGERTSE GFFKTKAGLD QAIARGLAYA PYADLIWCET SEPNMDEARR FAEAIHEQYP
     GKLLAYNCSP SFNWKRKLDD ETIANFQAEL GKMGYKFQFV TLAGFHALNH SMFELARAYK
     REGMAAYSRL QQSEFDSEEA GYTATRHQRE VGTGYFDEVS QVVTGGTSST TALKGSTETE
     QFTEEQLQN
//
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