ID   A0A1R4GL02_9MICO        Unreviewed;       299 AA.
AC   A0A1R4GL02;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE            EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN   ORFNames=FM112_13505 {ECO:0000313|EMBL:SJM68612.1};
OS   Gulosibacter sp. 10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Gulosibacter.
OX   NCBI_TaxID=1255570 {ECO:0000313|EMBL:SJM68612.1, ECO:0000313|Proteomes:UP000195931};
RN   [1] {ECO:0000313|EMBL:SJM68612.1, ECO:0000313|Proteomes:UP000195931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10(10) {ECO:0000313|Proteomes:UP000195931};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUIC01000036; SJM68612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4GL02; -.
DR   OrthoDB; 9771433at2; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000195931; Unassembled WGS sequence.
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:SJM68612.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195931}.
SQ   SEQUENCE   299 AA;  32844 MW;  02166C0ED2BE6F41 CRC64;
     MLYATNTAAA KRERFRARLA SGELLRMPGA FNPLSARLIE RKGFDGVYIS GAVLAADLGL
     PDIGLTTLTE IAARGRQIAR MTDLPALIDA DTGFGEPMNV ARTVQELEDA GLAGCHIEDQ
     VNPKRCGHLD GKSVVDVETA AKRIRAATDA RRDPNFLVMA RTDIRAAEGL DAAIDRAKAL
     VDAGADAIFP EAMRTLDEFA AMRAAVDVPL LANMTEFGKS ELFSVEQLRD VGMNLVIWPV
     SMLRISMGAT ERALDELAGE GHLREKLDEM QHRADLYDLV DYEDYNRFDT SVFNFRVDR
//