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

 H1S9M5_9BURK            Unreviewed;      1098 AA.
H1S9M5;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
28-MAR-2018, entry version 34.
RecName: Full=Fused isobutyryl-CoA mutase {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};
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};
Name=icmF {ECO:0000256|HAMAP-Rule:MF_02050};
ORFNames=OR16_23798 {ECO:0000313|EMBL:EHP40801.1};
Cupriavidus basilensis OR16.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Cupriavidus.
NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP40801.1, ECO:0000313|Proteomes:UP000005808};
[1] {ECO:0000313|EMBL:EHP40801.1, ECO:0000313|Proteomes:UP000005808}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR16 {ECO:0000313|EMBL:EHP40801.1,
ECO:0000313|Proteomes:UP000005808};
PubMed=22461549; DOI=10.1128/JB.06752-11;
Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
Nagy I., Horvath B., Nagy I., Kukolya J.;
"De Novo Genome Project of Cupriavidus basilensis OR16.";
J. Bacteriol. 194:2109-2110(2012).
-!- 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:EHP40801.1}.
-----------------------------------------------------------------------
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EMBL; AHJE01000058; EHP40801.1; -; Genomic_DNA.
RefSeq; WP_006160136.1; NZ_AHJE01000058.1.
ProteinModelPortal; H1S9M5; -.
EnsemblBacteria; EHP40801; EHP40801; OR16_23798.
PATRIC; fig|1127483.3.peg.4756; -.
OrthoDB; POG091H0B8X; -.
Proteomes; UP000005808; 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.
HAMAP; MF_02050; IcmF; 1.
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; 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};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000005808};
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}.
DOMAIN 28 158 B12-binding.
{ECO:0000259|PROSITE:PS51332}.
NP_BIND 221 226 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
NP_BIND 359 362 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
REGION 171 419 GTPase chaperone MeaI.
{ECO:0000256|HAMAP-Rule:MF_02050}.
COILED 465 492 {ECO:0000256|SAM:Coils}.
METAL 41 41 Cobalt (adenosylcobalamin axial ligand).
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 225 225 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 250 250 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 251 251 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 264 264 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 264 264 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 312 312 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 312 312 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 313 313 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 267 267 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 592 592 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 627 627 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 733 733 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 777 777 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 826 826 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 861 861 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 866 866 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 978 978 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 1097 1097 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
SEQUENCE 1098 AA; 121271 MW; 104C9C06A4FCC871 CRC64;
MTDLSDVQKG AQPSAPHPAQ GPKGPVNKVR FVTAASLFDG HDASINIMRR ILQSSGCEVI
HLGHNRSVDE VVNAALQEDV QGIAISSYQG GHVEYFKYMV DLLRQRGGEH IQLFGGGGGV
IVPLEIRELQ AYGVARIFSP EDGQRLGLAG MIADMVQRCD IDLARYAPTT LDAMKGGDRR
ALAQLITALE NGKADPALAD ALRAEAATVK TPVLGITGTG GAGKSSLTDE LIRRIRLDQR
DGLSIAVISI DPSRRKSGGA LLGDRIRMNA INHPRIFMRS LATREAGSEI SQALPDVLAA
CKVAGFDLII VETSGIGQGD AAIVAHVDLS LYVMTPEFGA ASQLEKIDML DFADFVAINK
FDRKGAQDAW RDVAKQVQRN REQWHAKPEE MPVYGTQASR FNDDGVTMLY QGLREALCAR
GMRAPAGVLP QLSGRISTGQ NVIVPPARNR YLAEIADTVR AYHRRVDAQS RLARERQQLR
EARRMLLAAS GQEDQGEALQ ALATEREAAL GGEERKLLAM WPEMRKAYSG DEYVVKIRDK
EIRTTLTTTT LSGTTVRKVV LPRFEDDGEV LKWLLRENVP GSFPYTAGVF AFKRENEDPT
RMFAGEGDAF RTNRRFKLVS EGMDAKRLST AFDSVTLYGE DPHTRPDIYG KVGNSGVSIA
TLDDMKVLYD GFDLTSPSTS VSMTINGPAP TILAMFMNTA IDQQLDKFRA DNNREPSADE
EAKIRAWVLQ NVRGTVQADI LKEDQGQNTC IFSTEFSLKV MGDIQAYFVH RQVRNFYSVS
ISGYHIAEAG ANPISQLAFT LSNGFTYVEA YLARGMDIDD FAPNLSFFFS NGMDPEYSVL
GRVARRIWAV TLRDKYGANE RSQKLKYHVQ TSGRSLHAQE IDFNDIRTTL QALIAIYDNC
NSLHTNAYDE AITTPTGESV RRALAIQLII NREWGVARCE NPNQGSFLID ELTDLVEEAV
MQEFERIAER GGVLGAMETG YQRGKIQEES LYYEQRKHDG TLPIIGVNTF RNPDGDPTHK
SLELARSSEE EKQGQLARLA DFQARHADAA PAMLQRLRQA VIDNDNVFAV LMDAVRVCSL
GQVTHALFEV GGQYRRNM


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