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Fused isobutyryl-CoA mutase [Includes: Isobutyryl-CoA mutase (ICM) (EC 5.4.99.13); p-loop GTPase (EC 3.6.5.-) (G-protein chaperone)]

 A0A0A3J6B9_9BACI        Unreviewed;      1090 AA.
A0A0A3J6B9;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
25-OCT-2017, entry version 19.
RecName: Full=Fused isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
Includes:
RecName: Full=Isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
Short=ICM {ECO:0000256|HAMAP-Rule:MF_02050};
EC=5.4.99.13 {ECO:0000256|HAMAP-Rule:MF_02050};
Includes:
RecName: Full=p-loop GTPase {ECO:0000256|HAMAP-Rule:MF_02050};
EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_02050};
AltName: Full=G-protein chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
Name=icmF {ECO:0000256|HAMAP-Rule:MF_02050};
ORFNames=CD30_01225 {ECO:0000313|EMBL:KGR92461.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR92461.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR92461.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR92461.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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. {ECO:0000256|HAMAP-Rule:MF_02050}.
-!- CATALYTIC ACTIVITY: 2-methylpropanoyl-CoA = butanoyl-CoA.
{ECO:0000256|HAMAP-Rule:MF_02050}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
{ECO:0000256|HAMAP-Rule:MF_02050}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
-!- COFACTOR:
Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02050}.
-!- 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).
{ECO:0000256|HAMAP-Rule:MF_02050}.
-!- SIMILARITY: Belongs to the IcmF family. {ECO:0000256|HAMAP-
Rule:MF_02050}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02050}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR92461.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000001; KGR92461.1; -; Genomic_DNA.
RefSeq; WP_036171224.1; NZ_JPVQ01000001.1.
EnsemblBacteria; KGR92461; KGR92461; CD30_01225.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
GO; GO:0047727; F:isobutyryl-CoA mutase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
GO; GO:0034784; F:pivalyl-CoA mutase activity; IEA:InterPro.
GO; GO:0006637; P:acyl-CoA metabolic process; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.240; -; 1.
HAMAP; MF_02050; IcmF; 1.
InterPro; IPR006159; Acid_CoA_mut_C.
InterPro; IPR016176; Cbl-dep_enz_cat.
InterPro; IPR006158; Cobalamin-bd.
InterPro; IPR036724; Cobalamin-bd_sf.
InterPro; IPR033669; IcmF.
InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
InterPro; IPR006098; MMCoA_mutase_a_cat.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF02310; B12-binding; 1.
Pfam; PF01642; MM_CoA_mutase; 1.
SUPFAM; SSF51703; SSF51703; 1.
SUPFAM; SSF52242; SSF52242; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
PROSITE; PS51332; B12_BINDING; 1.
3: Inferred from homology;
Chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
Cobalamin {ECO:0000256|HAMAP-Rule:MF_02050};
Cobalt {ECO:0000256|HAMAP-Rule:MF_02050};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_02050};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_02050};
Isomerase {ECO:0000256|HAMAP-Rule:MF_02050};
Magnesium {ECO:0000256|HAMAP-Rule:MF_02050};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_02050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_02050};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02050};
Reference proteome {ECO:0000313|Proteomes:UP000030595}.
DOMAIN 19 149 B12-binding.
{ECO:0000259|PROSITE:PS51332}.
NP_BIND 213 218 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
NP_BIND 350 353 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 32 32 Cobalt (adenosylcobalamin axial ligand).
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 217 217 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 241 241 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 242 242 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 255 255 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 255 255 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 303 303 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 303 303 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 304 304 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 258 258 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 582 582 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 617 617 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 723 723 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 767 767 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 816 816 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 851 851 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 856 856 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 968 968 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 1089 1089 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
SEQUENCE 1090 AA; 122579 MW; 1CE2C29D92487495 CRC64;
MVKLEKEQAE LGVYRPKHHV RFVTASSLFD GHDVSVNIMR RILQASGAEV IHLGHNRSVE
EVVNTAIQED AQGIAVSSYQ GGHMEYFKYM YDLLQQKGAP HIKIYGGGGG VILPREIKEL
HEYGIAGIFS PEDGMKLGLQ GMINKQIEGA DFSTLTGNYL ELLNELSTER PEIVANLITA
AEIGGSEEIA QLIIEAKKIA QKTPVIGITG TGGAGKSSLT DELILRFLRE FPDKKVAIIS
VDPTKQKTGG ALLGDRIRMN AIFNDRVYMR SLATRGSRTE LSDSIGDVLT IVKAAGYDLI
IVETSGIGQG DAEITKYTDL SMYVMTSEFG APTQLEKIDM IDYADLIVIN KFEKKGSEDA
LRQVQKQYQR SHGLWNESLD RMPVYGTIAS QFNDKGTNAL FAALISKINE KLQYNWQTSF
DQFVKTQKQD VIIPNNRRYY LREIAETVRN YHKHAAQQVE LARKLYQLEG TIETVRTQTP
DADALLASLT SLAEGVKSQL TQQSIRIIEN WEKLKEAYSG DEFVTKVRDK EIRTILTTTS
LSGTKIPKIS LPKFKDYGEI LRWVYAENVP GEFPYTAGVF PFKREGEDPK RQFAGEGTPE
RTNKRFHYLS KDDDAKRLST AFDSVTLYGE DPDYRPDIYG KVGESGVSVC TLEDMKKLYD
GFDLCAPSTS VSMTINGPAP IILAMFLNTA IDQQVRQKEQ ELGRPLSLDE FTEVREKTLQ
VVRGTVQADI LKEDQGQNTC IFSTEFALRM MGDIQQYFID HKVRNYYSVS ISGYHIAEAG
ANPISQLAFT LANGFTYVEY YLSRGMNIDD FAPNLSFFFS NGLDPEYTVI GRVARRIWSI
VMRDKYGANE RSQKLKYHIQ TSGRSLHAQE MDFNDIRTTL QALMALQDNC NSLHTNAYDE
AITTPTEESV RRAMAIQLII TKEHGLSKNE NPMQGAFIIE ELTDLVEQAV LDEFERINDR
GGVLGAMETQ YQRGKIQEES MYYEQLKHTG QLPIIGVNTY LNPNPKTEEE INSLQVARAS
KEEKELQIHN LRDFQKTHEG KCEEALNKLK EVALSGGNIF AQLMETVRVA SLGQITKALY
EVGGKYRRNM


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