ID A0A1L6HSR9_9BURK Unreviewed; 1195 AA.
AC A0A1L6HSR9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BTO02_01910 {ECO:0000313|EMBL:APR34366.1};
OS Paraburkholderia sp. SOS3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR34366.1, ECO:0000313|Proteomes:UP000184708};
RN [1] {ECO:0000313|EMBL:APR34366.1, ECO:0000313|Proteomes:UP000184708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SOS3 {ECO:0000313|EMBL:APR34366.1,
RC ECO:0000313|Proteomes:UP000184708};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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DR EMBL; CP018811; APR34366.1; -; Genomic_DNA.
DR RefSeq; WP_075155580.1; NZ_CP018811.1.
DR AlphaFoldDB; A0A1L6HSR9; -.
DR STRING; 1926494.BTO02_01910; -.
DR KEGG; para:BTO02_01910; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000184708; Chromosome 1.
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: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; IPR027417; P-loop_NTPase.
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 45..183
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
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 278..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 282
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 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 321
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 324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 373
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 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 420..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 685
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 720
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 830
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 874
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 923
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 958
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 963
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1075
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1195 AA; 130078 MW; 24F116C2E04ADD58 CRC64;
MTDLSTPQRA GGAALSDEAP ASESPPRAVQ PGQSSARGQR ARPARLRFVT AAALFDGHDA
SINIIRRMLQ ASGVEVIHLG HNRSVEEVAT AALQEDADGV AVSSYQGGHV EYFRYLVDLL
RARAGERIKV FGGGGGVIVP DEIAELERYG VERIYSPHDG QRLGLQGMID DMIARCADAA
RDEPQGEQMA QRSALQLAGE IAQALTTDLA RSDAPKHAGS AAERAADSNG AVFRKLARLI
THLETGTDAA ATAALSAAVA PHAHAARVPV LGITGTGGAG KSSLTDELIR RFRLDYDDAL
TIAVLAIDPS RRKSGGALLG DRIRMNAIGD WGAGSRVFMR SMATREASSE ISDALPAAID
ACKAAGFDLI VVETSGIGQG DAAIVPHVDK SLYVMTPEFG AASQLEKIDM LDFADFVAIN
KFDRKGAADA LRDVAKQVQR NRGEFSTAPA GMPVFGTIAS RFNDDGVTAL YQRVARALRA
RGLREGRARL PLLDGVRHSS GRHAIVPPER VRYLSDVAQT VRDYRARAEA QARIARERWQ
LIETRRMLAG GTSEPANSAA ASSQAGVRAM DPSTVASQDR GTSTNPATNP AIDTLIAART
AQLGEREKAL LDTWPHTVAA YSGDEHVVKI RDREIRTALT VETLSGNAIR KVSLPKYTDP
GEILRWLMLE NLPGYFPYTA GVFPFKRENE DPTRMFAGEG DPFRTNRRFR LLSAGMPAKR
LSTAFDSVTL YGEEPHERPD IYGKVGNSGV SVATLDDMKA LYDGFDLCAP DTSVSMTING
PAPAILAMFF NVAIDQQIER AREHARQAGR EPLSDEALEA ARRTALENAR GTVQADILKE
DQGQNTCIFS TEFSLKVMGD IQAYFVEYGV RNFYSVSISG YHIAEAGANP ISQLAYTLAN
GFTYVEAYLA RGMSIDDFAP NLSFFFSNGM DPEYTVLGRV ARRIWSVALR ERYGANERSQ
KLKYHVQTSG RSLHAQEIDF NDIRTTLQAL IAIYDNCNSL HTNAFDEAIT TPTEDSVRRA
VAIQLIINRE WGLAKSQNPN QGSFVIDELT DLVEAAVLAE FDRLTERGGV LGAMETGYQR
GRIQDESMLY EHRKHDGSYP IVGVNTFLGA HPHEAPPPIA LARSTEDEKQ SQLERLRAFQ
ARHRDAAPAA LERLRQAVID DRNVFAVLMD AVRVCSLGQV THALFEVGGQ YRRNM
//
