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Annotation rule MF_02050
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General rule information [?]

Accession MF_02050
Dates 6-JAN-2016 (Created)
20-NOV-2019 (Last updated, Version 3)
Name IcmF
Templates Q1LRY0 (ICMF_CUPMC); Q5Z110 (ICMF_NOCFA); Q5KUG0 (ICMF_GEOKA); Q146L7 (ICMF_PARXL): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Fused isobutyryl-CoA mutase;
RecName: Full=Isobutyryl-CoA mutase;
RecName: Full=P-loop GTPase;
EC 3.6.5.-;
AltName: Full=G-protein chaperone;
Gene name

Comments [?]

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
RHEA:19669: GTP + H2O = GDP + H(+) + phosphate
Cofactor adenosylcob(III)alamin
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 [?]

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; trigger=PRU00666;
Pfam PF02310; B12-binding; 1;
PF01642; MM_CoA_mutase; 1;
TIGRFAMs TIGR00641; acid_CoA_mut_N; 1;
TIGR00640; acid_CoA_mut_C; 1;

Features [?]

Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     219     224       GTP     G-[AS]-G-K-S-[ST]  
NP_BIND     357     360       GTP     N-K-x-[DE]  
REGION     169     417       GTPase chaperone MeaI        
REGION     418     579       Linker        
METAL     39     39       Cobalt (adenosylcobalamin axial ligand)     H  
METAL     223     223       Magnesium 1; catalytic     S  
METAL     248     248       Magnesium 2; via carbonyl oxygen     [IV]  
METAL     249     249       Magnesium 2     D  
METAL     262     262       Magnesium 1; catalytic     D  
METAL     262     262       Magnesium 2     D  
METAL     310     310       Magnesium 1; catalytic     E  
METAL     310     310       Magnesium 2     E  
METAL     311     311       Magnesium 2; via carbonyl oxygen     T  
BINDING     265     265       GTP     R  
BINDING     587     587       Substrate; via carbonyl oxygen     F  
BINDING     622     622       Substrate     R  
BINDING     728     728       Substrate     R  
BINDING     772     772       Substrate     Y  
BINDING     821     821       Substrate     S  
BINDING     856     856       Substrate     R  
BINDING     861     861       Substrate     K  
BINDING     973     973       GTP     E  
BINDING     1092     1092       GTP     N  

Additional information [?]

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.