ID I0JQ93_HALH3 Unreviewed; 431 AA.
AC I0JQ93;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 OrderedLocusNames=HBHAL_3971 {ECO:0000313|EMBL:CCG46313.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG46313.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG46313.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
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; HE717023; CCG46313.1; -; Genomic_DNA.
DR RefSeq; WP_014644202.1; NC_017668.1.
DR AlphaFoldDB; I0JQ93; -.
DR STRING; 866895.HBHAL_3971; -.
DR KEGG; hhd:HBHAL_3971; -.
DR PATRIC; fig|866895.3.peg.2998; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_019214_2_0_9; -.
DR Proteomes; UP000007397; 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:CCG46313.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 308..312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 431 AA; 47882 MW; 2CD16E3E1144664E CRC64;
MMNERVEKLR NKWQEEERWS SVLRPYEPED VIRLRGSMDI QHTLAEKGAE KLWNLLHEED
YVHALGALTG NQAMQQVKAG LKAIYLSGWQ VAADANLSGH MYPDQSLYPA NSVPQVVKRI
NQALQRADQI HHMEGKHDID WFAPIVADAE AGFGGQLNVF ELMKGMIEAG ASAVHFEDQL
SSEKKCGHLG GKVLLPTQTA VRNLISARFA ADVMGVPTII IARTDANAAD LITSDVDGSD
AEFLTGERTA EGFYKTKAGI DQAIARGLAY APYADLVWCE TSEPNIEEAR RFAEAIHEKF
PGKLLAYNCS PSFNWKKKLD DETIASFQRT LGEMGYKFQF VTLAGFHALN HGMFELARQY
KDRGMEAYSE LQQAEFSSEV YGYSATRHQR EVGTGYFDEV AQIISGGTSS TTALKGSTES
EQFTTETVSQ S
//
