HAMAP rule MF

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

HAMAP; MF_02050 (Get profile general information and statistics)

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

icmF

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.

Chaperone
Cobalamin
Cobalt
GTP-binding
Hydrolase
Isomerase
Magnesium
Metal-binding
Multifunctional enzyme
Nucleotide-binding

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.

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;

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

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.

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HAMAP rule MF_02050