ID A0A1A9NC19_9BURK Unreviewed; 1175 AA.
AC A0A1A9NC19;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Fused isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
DE Includes:
DE RecName: Full=Isobutyryl-CoA mutase {ECO:0000256|HAMAP-Rule:MF_02050};
DE Short=ICM {ECO:0000256|HAMAP-Rule:MF_02050};
DE EC=5.4.99.13 {ECO:0000256|HAMAP-Rule:MF_02050};
DE Includes:
DE RecName: Full=P-loop GTPase {ECO:0000256|HAMAP-Rule:MF_02050};
DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_02050};
DE AltName: Full=G-protein chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
GN Name=icmF {ECO:0000256|HAMAP-Rule:MF_02050};
GN ORFNames=A6V37_00080 {ECO:0000313|EMBL:OAJ63940.1};
OS Paraburkholderia ginsengiterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ63940.1, ECO:0000313|Proteomes:UP000078116};
RN [1] {ECO:0000313|EMBL:OAJ63940.1, ECO:0000313|Proteomes:UP000078116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY85 {ECO:0000313|EMBL:OAJ63940.1,
RC ECO:0000313|Proteomes:UP000078116};
RA Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible interconversion of isobutyryl-CoA
CC and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase
CC activity, associated with its G-protein domain (MeaI) that functions as
CC a chaperone that assists cofactor delivery and proper holo-enzyme
CC assembly. {ECO:0000256|HAMAP-Rule:MF_02050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA = butanoyl-CoA; Xref=Rhea:RHEA:13141,
CC ChEBI:CHEBI:57338, ChEBI:CHEBI:57371; EC=5.4.99.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02050};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02050};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|HAMAP-Rule:MF_02050};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02050}.
CC -!- DOMAIN: Is composed of four functional domains: the N-terminal 5'-
CC deoxyadenosylcobalamin binding region that is homologous to the small
CC subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely
CC acts as a chaperone for ICM, a structured linker region involved in
CC dimer formation, and a C-terminal part that is homologous to the large
CC substrate-binding subunit of ICM (IcmA). {ECO:0000256|HAMAP-
CC Rule:MF_02050}.
CC -!- SIMILARITY: Belongs to the IcmF family. {ECO:0000256|HAMAP-
CC Rule:MF_02050}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02050}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAJ63940.1}.
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DR EMBL; LXKA01000110; OAJ63940.1; -; Genomic_DNA.
DR RefSeq; WP_064266778.1; NZ_LXKA01000110.1.
DR AlphaFoldDB; A0A1A9NC19; -.
DR STRING; 1462993.A6V36_00890; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000078116; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047727; F:isobutyryl-CoA mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR GO; GO:0034784; F:pivalyl-CoA mutase activity; IEA:InterPro.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_02050; IcmF; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR033669; IcmF.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR43087:SF1; LAO_AO TRANSPORT SYSTEM ATPASE; 1.
DR PANTHER; PTHR43087; LYSINE/ARGININE/ORNITHINE TRANSPORT SYSTEM KINASE; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF03308; MeaB; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_02050};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|HAMAP-Rule:MF_02050};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_02050};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_02050};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02050};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02050};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02050};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02050};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_02050};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02050}.
FT DOMAIN 20..158
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 555..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 256..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 398..401
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 669
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 704
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 810
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 854
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 903
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 938
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 943
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1055
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1175 AA; 128111 MW; 6369B48A136E7A29 CRC64;
MTDLSTPQRA GSHKLPAGRR LRFVTAAALF DGHDASINIM RRILQASGVE VIHLGHNRSV
AEVASAALQE DADGVAVSSY QGGHNEYFRY LIDLLRARGG ERIKVFGGGG GVIVPEEIAE
LERYGVERIY SPQDGQRLGL QGMIDDMIAR CAEGARAATA TGASPIGEWI AEFAERRLPR
FDSHHDAAND AANEVANEVG NSAASTTDAA SFTFRRLAQL ISAFEAGGID PAGRDKLSAL
AQVARTPILG ITGTGGAGKS SLTDELIRRF RLDYGDTLAI AVLAIDPSRR KSGGALLGDR
IRMNAIGDWG GGPRVYLRSM ATREASSEIS DALPDALMLC KAAGFDLIVV ETSGIGQGDA
AIVPFVDESL YVMTPEFGAA SQLEKIDMLD FADFVAINKF DRQGAPDALR DVAKQVQRNR
GEFGKAPETM PVFGTIASRF NDDGVTALYR HVAAALGKHG LRAGHGRLTA PEALRCSSDR
HAIVPPARVR YLSDITQTVH AYRERADAQA RVARERWQLI EARRMLAEAR VGASAGASAS
SGASSAAAGS ATRTASATSA SSTTSTGSSD HALPQLDTLI EQRTALLGER ERHLLDAWPQ
TVAAYAGAEH IVRIRDREIR TALTVTTLSG SEVRKVSLPK FVDHGEILRW LMLDNLPGYF
PFTAGVFPFR RENEDPTRMF AGEGDPQRTN RRFKLLSEGM PAKRLSTAFD SVTLYGEEPH
ERPDIYGKVG NSGVSVATLD DMKALYDGFD LCAPETSVSM TINGPAPTIL AMFFNVAIDQ
QIARMTQQQG RPLTDDELAA TRRTALENVR GTVQADILKE DQGQNTCIFS TEFSLKVMGD
IQAYFVEHGV RNFYSVSISG YHIAEAGANP ISQLAYTLAN GFTYVEAYLA RGMSIDDFAP
NLSFFFSNGM DPEYTVLGRV ARRIWAVAMR ERYGANERSQ KLKYHVQTSG RSLHAQEIDF
NDIRTTLQAL IAIYDNCNSL HTNAFDEAIT TPTEESVRRA VAIQLIINRE WGLAKNQNPN
QGSFVIEELT DLVEEAVLAE FDRLTERGGV LGAMETGYQR GRIQDESMLY EHRKHDGSYP
IVGVNTFLSA HPHEAPPPIA LARSTEDEKQ SQLTRLHAFQ ARHREAAPAA LERLKRAVID
DDNVFAALMD VVRVCSLGQI THALFEVGGQ YRRNM
//
