HAMAP logo
Due to maintenance work, this service will be unavailable from Mon Nov 11 17:30 until Tue Nov 12 09:00 CET. Apologies for the inconvenience.

HAMAP rule MF_02050

Send feedback

General rule information [?]

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 [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONCatalyzes 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;
SUBUNITHomodimer.
DOMAINIs 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).
SIMILARITYBelongs to the IcmF family.

Keywords [?]


Gene Ontology [?]

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 [?]

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 [?]

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 [?]

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.



View rule in raw text format (no links)