ID A0A364Y2M5_9BACT Unreviewed; 429 AA.
AC A0A364Y2M5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DQQ10_11965 {ECO:0000313|EMBL:RAW00949.1};
OS Pseudochryseolinea flava.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Pseudochryseolinea.
OX NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAW00949.1, ECO:0000313|Proteomes:UP000251889};
RN [1] {ECO:0000313|EMBL:RAW00949.1, ECO:0000313|Proteomes:UP000251889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDU1-6 {ECO:0000313|EMBL:RAW00949.1,
RC ECO:0000313|Proteomes:UP000251889};
RA Li Y., Wang J.;
RT "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT isolated from soil.";
RL Submitted (JUN-2018) 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:RAW00949.1}.
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DR EMBL; QMFY01000005; RAW00949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364Y2M5; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000251889; 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:RAW00949.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000251889}.
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 180..181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 301..305
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 429 AA; 47495 MW; 4EDA329944E23C64 CRC64;
MNNIESMNNS RWKNIIRPYT QEQVTRLRGS VKIDYTLATL GARRLWNLLN EEHYVSALGA
LTGNQAVQQV QAGLKAIYLS GWQVAADANH SGQMYPDQSL YPADSVPGVV RRINNALIRA
DQLQTLHQDG NVHWMAPIIA DAEAGFGGNL NAFELMKMMI DAGAAAVHFE DQLSSAKKCG
HMGGKVLVPT REAIDKLVAA RLAADVLDVP TLIIARTDAD AATLITSDID DRDKPFIYGQ
RTVEGFYHVR NGIEQAISRG LSYAPYADLI WCETSYPDLV QAKRFAEAIH EKFPGKLLAY
NCSPSFNWAA KLSPDEMLHF RESLAALGYK FQFITLAGFH SLNTSMFELA LAYTEKGMLG
YSELQQREFS LQDEHGFKAV RHQAFVGTGY FDKVQEVVTA GSASTTAMKN STEEAQFETP
DKIKLELSA
//
