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 | Bacteria |
Templates | Q1LRY0 (ICMF_CUPMC); Q5Z110 (ICMF_NOCFA); Q5KUG0 (ICMF_GEOKA); Q146L7 (ICMF_PARXL): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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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 | RHEA:13141: 2-methylpropanoyl-CoA = butanoyl-CoA
EC 5.4.99.13 |
RHEA:19669: GTP + H2O = GDP + H(+) + phosphate | |
Cofactor | adenosylcob(III)alamin |
Mg(2+) | |
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
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.
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; trigger=PRU00666; |
Pfam | PF02310; B12-binding; 1; |
PF01642; MM_CoA_mutase; 1; | |
NCBIfam | TIGR00641; acid_CoA_mut_N; 1; |
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 | GTPase chaperone MeaI | |||||||||
REGION | 418 | 579 | 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 | None |
Comments | In many AdoCbl-dependent isomerases, e.g. methylmalonyl-CoA mutase (MCM), the G-protein chaperone is a separate protein. |