AC   MF_00743;
DC   Protein; auto
TR   HAMAP; MF_00743; -; 1; level=0
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Names: FumaraseC
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ID   FUMC
DE   RecName: Full=Fumarate hydratase class II;
DE            Short=Fumarase C;
DE            EC=4.2.1.2;
DE   AltName: Full=Aerobic fumarase;
DE   AltName: Full=Iron-independent fumarase;
GN   Name=fumC;
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CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC       site, and the non-catalytic B site that may play a role in the transfer
CC       of substrate or product between the active site and the solvent.
CC       Alternatively, the B site may bind allosteric effectors.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily.
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DR   Pfam; PF10415; FumaraseC_C; 1; trigger=no
DR   Pfam; PF00206; Lyase_1; 1; trigger=no
DR   PRINTS; PR00149; FUMRATELYASE; 1; trigger=no
DR   NCBIfam; TIGR00979; FumC_II; 1; trigger=no
DR   PROSITE; PS00163; FUMARATE_LYASES; 1; trigger=no
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KW   Cytoplasm
KW   Lyase
KW   Tricarboxylic acid cycle
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GO   GO:0004333; F:fumarate hydratase activity
GO   GO:0006099; P:tricarboxylic acid cycle
GO   GO:0005737; C:cytoplasm
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FT   From: FUMC_MYCTU (P9WN93)
FT   BINDING         104..106
FT                   /ligand="substrate"
FT   Condition: S-x-T
FT   BINDING         128..131
FT                   /ligand="substrate"
FT                   /note="in site B"
FT   Condition: [HN]-x-N-D
FT   BINDING         138..140
FT                   /ligand="substrate"
FT   Condition: S-[ST]-N
FT   BINDING         324..326
FT                   /ligand="substrate"
FT   Condition: K-x-N
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT   Condition: H
FT   ACT_SITE        318
FT   Condition: S
FT   BINDING         186
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         319
FT                   /ligand="substrate"
FT   Condition: S
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT   Condition: E
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Size: 438-484;
Related: None;
Template: P05042; P9WN93; P39461;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BRADU, PSEAE
Plasmid: in RALN1
Comments: None
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# Revision 1.32 2023/11/28
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