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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)]

 A0A1Q6A2K6_9SPHI        Unreviewed;      1311 AA.
A0A1Q6A2K6;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
25-OCT-2017, entry version 6.
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=RG47T_3719 {ECO:0000313|EMBL:OKS88254.1};
Mucilaginibacter polytrichastri.
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Mucilaginibacter.
NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS88254.1, ECO:0000313|Proteomes:UP000186720};
[1] {ECO:0000313|EMBL:OKS88254.1, ECO:0000313|Proteomes:UP000186720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RG4-7 {ECO:0000313|EMBL:OKS88254.1,
ECO:0000313|Proteomes:UP000186720};
Li Y.;
"Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
isolated from the moss sample.";
Submitted (NOV-2016) 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:OKS88254.1}.
-----------------------------------------------------------------------
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EMBL; MPPL01000001; OKS88254.1; -; Genomic_DNA.
Proteomes; UP000186720; 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: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; IPR016176; Cbl-dep_enz_cat.
InterPro; IPR006158; Cobalamin-bd.
InterPro; IPR036724; Cobalamin-bd_sf.
InterPro; IPR007569; DUF559.
InterPro; IPR033669; IcmF.
InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011335; Restrct_endonuc-II-like.
Pfam; PF02310; B12-binding; 1.
Pfam; PF04480; DUF559; 1.
Pfam; PF01642; MM_CoA_mutase; 2.
SUPFAM; SSF51703; SSF51703; 2.
SUPFAM; SSF52242; SSF52242; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF52980; SSF52980; 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:UP000186720};
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:UP000186720}.
DOMAIN 12 150 B12-binding.
{ECO:0000259|PROSITE:PS51332}.
NP_BIND 208 213 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
NP_BIND 344 347 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 25 25 Cobalt (adenosylcobalamin axial ligand).
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 212 212 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 235 235 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 236 236 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 249 249 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 249 249 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 297 297 Magnesium 1; catalytic.
{ECO:0000256|HAMAP-Rule:MF_02050}.
METAL 297 297 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02050}.
METAL 298 298 Magnesium 2; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 252 252 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 631 631 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 946 946 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 990 990 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 1039 1039 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 1074 1074 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 1079 1079 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02050}.
BINDING 1191 1191 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
BINDING 1310 1310 GTP. {ECO:0000256|HAMAP-Rule:MF_02050}.
SEQUENCE 1311 AA; 146993 MW; E43850197A80A122 CRC64;
MENVPVYKNT YKIRFVTAAS LFDGHDATIN IMRRILQSSG AEVIHLGHNR SVDEVVNCAI
QEDVQGIALT SYQGGHIEYF KYMHDLLKER GAGHIKIFGG GGGVFLPKEI EELQAYGISK
IYSPDDGRRM GLQGMINDML QQCDFETKVT LNGEMKHLPQ KDAKAIAQLI TLAENHYEQL
PKSITAPSAS DKTANKAIPV LGITGTGGSG KSSLVDEIVR RFLAETDKTM AIISVDPSKR
KTGGALLGDR IRMNAINNPR IYMRSLATRQ ANLALSGYVQ ESINICKAAG FDLIIVETSG
IGQSDTMITD YCDVTLYVMT PEFGAATQLE KIDMLDFADL VAVNKFDKRG ALDAIRDVRR
QYKRNHLLFD ASDDSMPVFG TMASQFNDPG MNSLFDALMK TIAAKTGIDF HPNLPEQTIE
QDKIYIIPPD RIRYLAEIAE SSVAYTTWVN EQCKIAKQLF MVKGTMDLLA ENTSLKEHTP
NPSQEGKNLT PTLSKGDGVK DGLQEIYQYL EDHLYPDCKR LLKEWPDTIQ KYKADNFIYK
VRDKEIKQPL FSTSLSQLRI PKISLPKYEA WGDVLRWLLT ENLPGEFPYA AGVFPLKREG
EDPTRMFAGE GGPERTNKRF HYVSLGQPAH RLSTAFDSVT LYGEDPHIRP DIYGKIGNAG
VSIATLDDAK KLYSGFDLCS PSTSVSMTIN GPAPMLLGFF MNAAIDQQCE KYIIENKLEY
LVEAKFKEFY DDKGLERPVY VSSSTVKASP QPSPEERGQN DRGYKTADTR IWEILKSNSR
DNRKNQTEAE NILWQQLRNS KTKYKIRRQH AVDGYIADFI CLSKGLIIEV DGGYHDFTVE
QDEVRTAILK EEGFDVIRFT NDEVINDTEN VIKKITLTLN TQQDKKTQTF ISNSLSPGEG
WGEAKQASLP EGNNGLGLLL LGLTGDQILP PDTYAKIKAY AIANVRGTVQ ADILKEDQAQ
NTCIFSTEFA LRLMGDIQQY FIDEKVRNFY SVSISGYHIA EAGANPVTQL AFTLANGFTY
VEYYLSRGMN IDDFAPNLSF FFSNGIDPEY SVIGRVARRI WAKAIKNKYK GNDRSQKLKY
HIQTSGRSLH AQEIDFNDIR TTLQALYAIY DNCNSLHTNA YDEAITTPTE ESVRRAMAIQ
LIINRELGLT KNENPIQGAF IIEELTDLVE EAVLAEFKRI NDRGGVLGAM ETMYQRSKIQ
EESLYYETLK HTGEFPIIGV NTFLNKKGSP TLVPAEVIRA TEEEKQLQIT TLEAFKQRNA
DKAPALLKTL QQTAVDGENT FEQLMDVCKY CSLGQISNAL YAVGGQYRRN M


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