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Database: UniProt
Entry: R8DG74_BACCE
LinkDB: R8DG74_BACCE
Original site: R8DG74_BACCE 
ID   R8DG74_BACCE            Unreviewed;       302 AA.
AC   R8DG74;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE            EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN   ORFNames=IGA_00038 {ECO:0000313|EMBL:EOO22837.1};
OS   Bacillus cereus HuA3-9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053205 {ECO:0000313|EMBL:EOO22837.1, ECO:0000313|Proteomes:UP000014003};
RN   [1] {ECO:0000313|EMBL:EOO22837.1, ECO:0000313|Proteomes:UP000014003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HuA3-9 {ECO:0000313|EMBL:EOO22837.1,
RC   ECO:0000313|Proteomes:UP000014003};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus HuA3-9.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the thermodynamically favored C-C bond cleavage of
CC       (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.
CC       {ECO:0000256|RuleBase:RU361121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC         succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC         Evidence={ECO:0000256|RuleBase:RU361121};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|RuleBase:RU361121}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Methylisocitrate lyase family. {ECO:0000256|ARBA:ARBA00009282,
CC       ECO:0000256|RuleBase:RU361121}.
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:EOO22837.1}.
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DR   EMBL; AHDZ01000001; EOO22837.1; -; Genomic_DNA.
DR   RefSeq; WP_002065269.1; NZ_KB976125.1.
DR   AlphaFoldDB; R8DG74; -.
DR   PATRIC; fig|1053205.3.peg.41; -.
DR   HOGENOM; CLU_027389_3_2_9; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000014003; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; 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; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR012695; PrpB.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR02317; prpB; 1.
DR   PANTHER; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU361121, ECO:0000313|EMBL:EOO22837.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   302 AA;  32850 MW;  53F42CE74B3B41E2 CRC64;
     MAWVVNKQST QEELANSFRA LVEANEILQI PGAHDAMAAL VAKNTGFSAL YLSGAAYTAS
     KGLPDLGIVT STEVAERARD LVRATDLPVL VDIDTGFGGV LNVARTAVEM VEAKVAAVQI
     EDQQLPKKCG HLNGKKLVTT EELVQKIKAI KEVAPSLYIV ARTDARGVEG LDASIERANA
     YVKAGADAIF PEALQSEEEF RLFNSKVNAP LLANMTEFGK TPYYSAEEFA NMGFQMVIYP
     VTSLRVAAKA YENVFTLIKE TGSQKDALSN MQTRSELYET ISYHDFEELD TGIAKTVLSE
     DQ
//
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