ID   A0A1G9CXM5_9MICO        Unreviewed;       303 AA.
AC   A0A1G9CXM5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Methylisocitrate lyase {ECO:0000256|RuleBase:RU361121};
DE            EC=4.1.3.30 {ECO:0000256|RuleBase:RU361121};
GN   ORFNames=SAMN05216282_1082 {ECO:0000313|EMBL:SDK56438.1};
OS   Cryobacterium psychrotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK56438.1, ECO:0000313|Proteomes:UP000198701};
RN   [1] {ECO:0000313|EMBL:SDK56438.1, ECO:0000313|Proteomes:UP000198701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK56438.1,
RC   ECO:0000313|Proteomes:UP000198701};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNFU01000008; SDK56438.1; -; Genomic_DNA.
DR   STRING; 386301.SAMN05216282_1082; -.
DR   OrthoDB; 9771433at2; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000198701; 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:SDK56438.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198701}.
SQ   SEQUENCE   303 AA;  32509 MW;  77A76A78B6CC71B3 CRC64;
     MLYAAATAAE KRLNLRAGLA SGTIQRFPGA FNPLSAKLIQ AKGFEGVYIS GAVLSADLGL
     PDIGLTTLTE VAGRAQQIAR MTDLPAIVDA DTGFGEPMNV ARTIQTLEDA GLAGMHIEDQ
     VNPKRCGHLD GKQVVDEETA LKRIRAAVDA RRDPNFLVMA RTDIRATVPG DGGLDAAVDR
     AKKLVDAGAD AIFPEAMATL AEFEAIRAAV DVPLLANMTE FGKSELFTVD QLAGIGINMV
     IWPVSLLRLA MGSAARGLDT LIGHGTLEPV LAEMQHRADL YELLDYESYN QFDTNVFNFQ
     IKR
//