ID M0F876_9EURY Unreviewed; 346 AA.
AC M0F876;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Isocitrate lyase and phosphorylmutase {ECO:0000313|EMBL:ELZ56150.1};
GN ORFNames=C466_04869 {ECO:0000313|EMBL:ELZ56150.1};
OS Halorubrum distributum JCM 10118.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227468 {ECO:0000313|EMBL:ELZ56150.1, ECO:0000313|Proteomes:UP000011614};
RN [1] {ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|Proteomes:UP000011614};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELZ56150.1, ECO:0000313|Proteomes:UP000011614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10118 {ECO:0000313|EMBL:ELZ56150.1,
RC ECO:0000313|Proteomes:UP000011614};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ56150.1}.
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DR EMBL; AOJN01000023; ELZ56150.1; -; Genomic_DNA.
DR RefSeq; WP_004599053.1; NZ_AOJN01000023.1.
DR AlphaFoldDB; M0F876; -.
DR PATRIC; fig|1227468.4.peg.935; -.
DR OrthoDB; 9667at2157; -.
DR Proteomes; UP000011614; Unassembled WGS sequence.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
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; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ELZ56150.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT REGION 310..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 346 AA; 38991 MW; 48605560FC615AFB CRC64;
MNPNELDDDV FDRDIDNPAG RKLRELFEEQ EYTFAPGIYH ALDARLAEMA GLDAAYMSGY
STVLGQFGFP DLEMVTMSEM VENAKRMVEA TNLPVVADCD TGYGGVHNVR RAVREYEKAG
VAAVHIEDQT SPKRCGHIAG KQIVSREQAR SRFEAAVDAK QSEDTVIIAR TDAYGSANGD
WEEHLERGRI YADAGVDLVW PEMPDPSRED AVEYAETIHE THPDLDLAFN YSSSFEWGAE
EDPLTFEELG DLGYQYIFIT LYGLHSGAHA AYEDFENIAE NDEEAQFDLE ERYIGHETES
HHELSFVPRY QDIEAEFDPE ARQRQEESAG FTEDENDPIT ASEGDD
//
