AC   MF_01939;
DC   Protein; auto
TR   HAMAP; MF_01939; -; 1; level=0
XX
Names: PrpB
XX
ID   PRPB
DE   RecName: Full=2-methylisocitrate lyase;
DE            Short=MICL;
DE            Short=2-MIC;
DE            EC=4.1.3.30;
DE   AltName: Full=(2R,3S)-2-methylisocitrate lyase;
GN   Name=prpB;
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CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the 2-methylcitrate cycle (propionate degradation route). Catalyzes
CC       the thermodynamically favored C-C bond cleavage of (2R,3S)-2-
CC       methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-
CC       carbanion intermediate.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Methylisocitrate lyase family.
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DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1; trigger=no
DR   NCBIfam; TIGR02317; prpB; 1; trigger=no
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KW   Lyase
KW   Magnesium
KW   Metal-binding
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GO   GO:0000287; F:magnesium ion binding
GO   GO:0046421; F:methylisocitrate lyase activity
GO   GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle
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FT   From: PRPB_ECOLI (P77541)
FT   BINDING         45..47
FT                   /ligand="substrate"
FT   Condition: S-x-[GA]
FT   BINDING         123..124
FT                   /ligand="substrate"
FT   Condition: C-G
FT   BINDING         210..212
FT                   /ligand="substrate"
FT   Condition: N-x-T
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         158
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         188
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         241
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         270
FT                   /ligand="substrate"
FT   Condition: R
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Size: 267-332;
Related: None;
Template: P77541; Q56062; Q937P0;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in CORGL
Plasmid: None
Comments: None
XX
# Revision 1.9 2023/06/01
//