ID A0A0A1CZW0_9MICC Unreviewed; 440 AA.
AC A0A0A1CZW0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ART_3158 {ECO:0000313|EMBL:AIY02757.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY02757.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY02757.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY02757.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
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};
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DR EMBL; CP007595; AIY02757.1; -; Genomic_DNA.
DR RefSeq; WP_038466056.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1CZW0; -.
DR STRING; 1494608.ART_3158; -.
DR KEGG; arm:ART_3158; -.
DR HOGENOM; CLU_019214_2_0_11; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000030301; Chromosome.
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:AIY02757.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 103..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 325..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 440 AA; 48002 MW; 43AA864B73CF7BEC CRC64;
MTAAFEPAKT PEQIRTEAVA ALELEWAANP RWEGVERSFS AADVIQLRGR VNEEHTLARR
GSEKLWNQLT SAAPGGYTNA LGALTGNQAV QQVKAGLKAI YLSGWQVAAD ANSNGNTYPD
QSLYPVDSVP KVVRRINNAL LRSDQIEFSE GLQTVEDWLV PIVADAEAGF GGPLNAYELM
KSMITSGAAG VHWEDQLASE KKCGHLGGKV LIPTAQHVRT LNAARLAADV AGVPSVIIAR
TDAEAATLIT SDVDERDQPF LTGERTAEGF YHVKNGLEPS IARARAYAPH SDLIWMETGT
PDLEHAKKFA EGVKSEFPDQ MLAYNCSPSF NWKKHLDDAT IAKFQRELGA MGYTFQFITL
AGFHSLNYSM FDLAHGYARN GMSSYVELQE REFDSESRGY TATKHQREVG TGYFDLVATA
LNPNSGTLAL AGSTEAQQFH
//
