ID A0A3N5CU77_9SPHN Unreviewed; 531 AA.
AC A0A3N5CU77;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN ORFNames=EG799_09280 {ECO:0000313|EMBL:RPF72783.1};
OS Aurantiacibacter spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2488860 {ECO:0000313|EMBL:RPF72783.1, ECO:0000313|Proteomes:UP000275232};
RN [1] {ECO:0000313|EMBL:RPF72783.1, ECO:0000313|Proteomes:UP000275232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E23 {ECO:0000313|EMBL:RPF72783.1,
RC ECO:0000313|Proteomes:UP000275232};
RA Zhuang L., Luo L.;
RT "Erythrobacter spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (NOV-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:RPF72783.1}.
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DR EMBL; RPFZ01000001; RPF72783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5CU77; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000275232; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RPF72783.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000275232}.
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 531 AA; 59078 MW; 91286387CE452998 CRC64;
MTYFEEIHRQ SAIRQKAGEG WSDIDPEFAA RLRVQNRFAT GLDIARHTAR IMRADMAAYD
ADPAAYTQSL GCWHGFIGQQ KMISIKKHFG TTRGRYLYLS GWMVAALRSE FGPLPDQSMH
EKTSVPALIA ELYTFLRQAD ARELGMLFRY LDAAREAGDE AAAARAQQAI DSHETHVVPI
IADIDAGFGN AEATYLLARK MIEAGACALQ IENQVSDEKQ CGHQDGKVTV PHEDFLQKIR
ACRYAFLELG VPDGVIVART DSLGAGLTKQ IAYSREPGDL GDRYNSFLDC EEIAPGQIGN
GQVLISRGGK LLEPKRLPSN LYRFRPGTGE DRVVLDCITS LQNGADLLWI ETEKPHVEQI
AGMVERIRAE VPGAKLVYNN SPSFNWTLNF RQQVYDAWAA EGRDMSDYDR ERLMSEHYDA
SELGREADER IRTFQADAAK RAGIFHHLIT LPTYHTAALS TDNLAKRYFG EDGMLGYVRQ
VQREEIRQGI ACVKHQNMAG SDIGDDHKEA FAGEAALKAG GAHNTMNQFA A
//