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Database: UniProt
Entry: A0A075JG44_9MICO
LinkDB: A0A075JG44_9MICO
Original site: A0A075JG44_9MICO 
ID   A0A075JG44_9MICO        Unreviewed;       427 AA.
AC   A0A075JG44;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   Name=aceA {ECO:0000313|EMBL:TJZ98612.1};
GN   ORFNames=FA951_01025 {ECO:0000313|EMBL:TJZ98612.1}, HX89_09675
GN   {ECO:0000313|EMBL:AIF41171.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF41171.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF41171.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF41171.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TJZ98612.1, ECO:0000313|Proteomes:UP000307824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA37 {ECO:0000313|EMBL:TJZ98612.1,
RC   ECO:0000313|Proteomes:UP000307824};
RA   Williams A.N., Maclea K.S.;
RT   "Genome sequence of Dermacoccus nishinomiyaensis strain TSA37.";
RL   Submitted (APR-2019) 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; CP008889; AIF41171.1; -; Genomic_DNA.
DR   EMBL; SUPQ01000001; TJZ98612.1; -; Genomic_DNA.
DR   RefSeq; WP_006944896.1; NZ_VECS01000001.1.
DR   AlphaFoldDB; A0A075JG44; -.
DR   STRING; 1274.HX89_09675; -.
DR   GeneID; 41841407; -.
DR   KEGG; dni:HX89_09675; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_11; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000027986; Chromosome.
DR   Proteomes; UP000307824; 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:AIF41171.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027986}.
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         91..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         192..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         313..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   427 AA;  47470 MW;  161D2E66BBA74C0F CRC64;
     MTGENIQARA AEIQKDWDTN ERWKNVKRDY SAEDVVRLQG SIQEEFTLAK HGAENLWEKL
     HTEDFVNALG ALTGNQAVQQ VKAGLKAIYL SGWQVAGDAN LAAQTYPDQS LYPANSVPQV
     VRRINNALMR ADQIEFSEGI KSVDEWLVPI VADAEAGFGG PLNAYELMKS MIAAGAAGVH
     WEDQLASEKK CGHLGGKVLI PTKQHVRTLN AARLATDVSN TPTVVIARTD AEAATLITSD
     VDERDQQFLT GERTNEGFYK VKNGIEPCIE RAKAYAPYAD LIWMETGTPD LELAKKFAES
     VKAEFPDQML AYNCSPSFNW KKHLDDDTIA KFQRELGAMG FKFQFITLAG FHALNYSMFD
     LAHGYAREQM KAYVELQERE FASESRGYTA TRHQREVGTG YFDLVATTLN PESSTTALKE
     STESAQF
//
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