AC MF_02050; DC Protein; auto TR HAMAP; MF_02050; -; 1; level=0 XX Names: IcmF XX ID ICMF DE RecName: Full=Fused isobutyryl-CoA mutase; DE Includes: DE RecName: Full=Isobutyryl-CoA mutase; DE Short=ICM; DE EC=5.4.99.13; DE Includes: DE RecName: Full=P-loop GTPase; DE EC=3.6.5.-; DE AltName: Full=G-protein chaperone; GN Name=icmF; XX CC -!- FUNCTION: Catalyzes the reversible interconversion of isobutyryl-CoA CC and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase CC activity, associated with its G-protein domain (MeaI) that functions as CC a chaperone that assists cofactor delivery and proper holo-enzyme CC assembly. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-methylpropanoyl-CoA = butanoyl-CoA; Xref=Rhea:RHEA:13141, CC ChEBI:CHEBI:57338, ChEBI:CHEBI:57371; EC=5.4.99.13; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC -!- COFACTOR: CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homodimer. CC -!- DOMAIN: Is composed of four functional domains: the N-terminal 5'- CC deoxyadenosylcobalamin binding region that is homologous to the small CC subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely CC acts as a chaperone for ICM, a structured linker region involved in CC dimer formation, and a C-terminal part that is homologous to the large CC substrate-binding subunit of ICM (IcmA). CC -!- SIMILARITY: Belongs to the IcmF family. XX DR PROSITE; PS51332; B12_BINDING; 1; trigger=yes DR Pfam; PF02310; B12-binding; 1; trigger=no DR Pfam; PF01642; MM_CoA_mutase; 1; trigger=no DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1; trigger=no DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1; trigger=no XX KW Chaperone KW Cobalamin KW Cobalt KW GTP-binding KW Hydrolase KW Isomerase KW Magnesium KW Metal-binding KW Multifunctional enzyme KW Nucleotide-binding XX GO GO:0031419; F:cobalamin binding GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity GO GO:0047727; F:isobutyryl-CoA mutase activity GO GO:0000287; F:magnesium ion binding GO GO:0006637; P:acyl-CoA metabolic process XX FT From: ICMF_CUPMC (Q1LRY0) FT BINDING 219..224 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: G-[AS]-G-K-S-[ST] FT BINDING 357..360 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: N-K-x-[DE] FT REGION 169..417 FT /note="GTPase chaperone MeaI" FT REGION 418..579 FT /note="Linker" FT BINDING 39 FT /ligand="adenosylcob(III)alamin" FT /ligand_id="ChEBI:CHEBI:18408" FT /ligand_part="Co" FT /ligand_part_id="ChEBI:CHEBI:27638" FT /note="axial binding residue" FT Condition: H FT BINDING 223 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: S FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: [IV] FT BINDING 249 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: D FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 310 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: E FT BINDING 310 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: E FT BINDING 311 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: T FT BINDING 265 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 587 FT /ligand="substrate" FT Condition: F FT BINDING 622 FT /ligand="substrate" FT Condition: R FT BINDING 728 FT /ligand="substrate" FT Condition: R FT BINDING 772 FT /ligand="substrate" FT Condition: Y FT BINDING 821 FT /ligand="substrate" FT Condition: S FT BINDING 856 FT /ligand="substrate" FT Condition: R FT BINDING 861 FT /ligand="substrate" FT Condition: K FT BINDING 973 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: E FT BINDING 1092 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: N XX Size: 1030-1300; Related: None; Template: Q1LRY0; Q5Z110; Q5KUG0; Q146L7; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: In many AdoCbl-dependent isomerases, e.g. methylmalonyl-CoA mutase (MCM), the G-protein chaperone is a separate protein. XX # Revision 1.6 2023/06/01 //