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HAMAP rule MF_02050
General rule information
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Accession | MF_02050 |
Dates | 6-JAN-2016 (Created)
1-JUN-2023 (Last updated, Version 6) |
Name | IcmF |
Scope(s) |
Bacteria |
Template(s) | Q1LRY0 (ICMF_CUPMC); Q5Z110 (ICMF_NOCFA); Q5KUG0 (ICMF_GEOKA); Q146L7 (ICMF_PARXL); [ Recover all ] |
Triggered by |
HAMAP; MF_02050 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ICMF |
Protein name | RecName: Full=Fused isobutyryl-CoA mutase; Includes: RecName: Full=Isobutyryl-CoA mutase; Short=ICM; EC=5.4.99.13; Includes: RecName: Full=P-loop GTPase; EC=3.6.5.-; AltName: Full=G-protein chaperone; |
Gene name | Name=icmF; |
Comments
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FUNCTION | Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. |
CATALYTIC ACTIVITY | Reaction=2-methylpropanoyl-CoA = butanoyl-CoA; Xref=Rhea:RHEA:13141, ChEBI:CHEBI:57338, ChEBI:CHEBI:57371; EC=5.4.99.13; |
CATALYTIC ACTIVITY | Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; |
COFACTOR | Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
SUBUNIT | Homodimer. |
DOMAIN | Is composed of four functional domains: the N-terminal 5'- deoxyadenosylcobalamin binding region that is homologous to the small subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely acts as a chaperone for ICM, a structured linker region involved in dimer formation, and a C-terminal part that is homologous to the large substrate-binding subunit of ICM (IcmA). |
SIMILARITY | Belongs to the IcmF family. |
Keywords
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Chaperone |
Cobalamin |
Cobalt |
GTP-binding |
Hydrolase |
Isomerase |
Magnesium |
Metal-binding |
Multifunctional enzyme |
Nucleotide-binding |
Gene Ontology
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GO:0031419; Molecular function:cobalamin binding |
GO:0005525; Molecular function:GTP binding |
GO:0003924; Molecular function:GTPase activity |
GO:0047727; Molecular function:isobutyryl-CoA mutase activity |
GO:0000287; Molecular function:magnesium ion binding |
GO:0006637; Biological process:acyl-CoA metabolic process |
Cross-references
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PROSITE | PS51332; B12_BINDING; 1; |
Pfam | PF02310; B12-binding; 1; |
Pfam | PF01642; MM_CoA_mutase; 1; |
NCBIfam | TIGR00641; acid_CoA_mut_N; 1; |
NCBIfam | TIGR00640; acid_CoA_mut_C; 1; |
Features
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From: ICMF_CUPMC (Q1LRY0) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 219 | 224 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
G-[AS]-G-K-S-[ST] | ||||||||
BINDING | 357 | 360 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
N-K-x-[DE] | ||||||||
REGION | 169 | 417 | /note="GTPase chaperone MeaI" | |||||||||
REGION | 418 | 579 | /note="Linker" | |||||||||
BINDING | 39 | 39 | /ligand="adenosylcob(III)alamin" /ligand_id="ChEBI:CHEBI:18408" /ligand_part="Co" /ligand_part_id="ChEBI:CHEBI:27638" /note="axial binding residue" |
H | ||||||||
BINDING | 223 | 223 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
S | ||||||||
BINDING | 248 | 248 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
[IV] | ||||||||
BINDING | 249 | 249 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
BINDING | 262 | 262 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
D | ||||||||
BINDING | 262 | 262 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
BINDING | 310 | 310 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
E | ||||||||
BINDING | 310 | 310 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
E | ||||||||
BINDING | 311 | 311 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
T | ||||||||
BINDING | 265 | 265 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
R | ||||||||
BINDING | 587 | 587 | /ligand="substrate" | F | ||||||||
BINDING | 622 | 622 | /ligand="substrate" | R | ||||||||
BINDING | 728 | 728 | /ligand="substrate" | R | ||||||||
BINDING | 772 | 772 | /ligand="substrate" | Y | ||||||||
BINDING | 821 | 821 | /ligand="substrate" | S | ||||||||
BINDING | 856 | 856 | /ligand="substrate" | R | ||||||||
BINDING | 861 | 861 | /ligand="substrate" | K | ||||||||
BINDING | 973 | 973 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
E | ||||||||
BINDING | 1092 | 1092 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" |
N |
Additional information
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Size range | 1030-1300 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | In many AdoCbl-dependent isomerases, e.g. methylmalonyl-CoA mutase (MCM), the G-protein chaperone is a separate protein. |