ID A0A1H6ADL1_9ACTN Unreviewed; 1075 AA.
AC A0A1H6ADL1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04489712_105365 {ECO:0000313|EMBL:SEG46462.1};
OS Thermomonospora echinospora.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=1992 {ECO:0000313|EMBL:SEG46462.1, ECO:0000313|Proteomes:UP000236723};
RN [1] {ECO:0000313|Proteomes:UP000236723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43163 {ECO:0000313|Proteomes:UP000236723};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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; FNVO01000005; SEG46462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ADL1; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000236723; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000236723}.
FT DOMAIN 10..148
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 400..561
FT /note="Linker"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT COILED 459..493
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 23
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 202..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 206
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 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 245
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 248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 292
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 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 339..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 569
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 604
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 710
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 754
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 803
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 838
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 843
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 955
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1074
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1075 AA; 117808 MW; C2EE8D407DA65615 CRC64;
MATLYKPVHP VRFVTAAALF DGHDAAINIM RRILQSQGAE VIHLGHNRSV AEIVEAAIQE
DAQGVAISSY QGGHVEFFRY LVDLLAERGA GHIKVYGGGG GVIVPEEIEL LHAHGVARIF
SPEDGQRLGL TGMINELIRD CDVDPAAGGL PGEGLTGGDV RALARAITVI EAGQADEDGL
RAVREAAAGR TVPVLGITGT GGSGKSSLTD ELVRRFRVDT EDKLRIAVIA VDPTRRRSGG
ALLGDRIRMN SLHEGTTFFR SLATRGAREL PEHLGDVIAA CQAAGYDLVI VETPGIGQGD
AAIVPFADVK LYVMTPEFGA ASQLEKIDML DFADAVAINK FERRGAEDAL RDVRRQLVRN
REAFGARPED MPVFGTIAAR FNDDGVTALY HELRERLAEH GLPAAPGALA RVPGRVSSRI
QAVIPPERAG YLAEIARTVA AYHAETEAQA EAARRRQRLR TARELLAEAG GDVAELERLL
AAAEEEVGDE ARALLDGWAE TRDAYSGDEL VVRVRDREIH TPLWRETLSG TRIPRVALPR
LSDDGDLLRF LRLENLPGMF PFTAGVFPFK RDDEDPTRMF AGEGDAFRTN RRFKRLSQGQ
PATRLSTAFD SVTLYGQDPA ERPDIYGKVG TSGVSIATLD DMKALYDGFD LTDPTTSVSM
TINGPAPTIL AFFLNTAIDQ AMERFATEHG REPSQQEAAE VRAAVLATVR GTVQADILKE
DQGQNTCIFS TEFSLRMMAD IQEWFVQNGV RNFYSVSISG YHIAEAGANP ISQLAFTLAN
GFTYVEAYLA RGMHIDDFAH NLSFFFSNGM DPEYSVLGRV ARRIWAIAMR ERYGASERGQ
KLKYHVQTSG RSLHAQEMDF NDIRTTLQAL IAIYDNCNSL HTNAYDEAIT TPTEESVRRA
LAIQLIINRE WGLAKNENPN QGSFIIEQLT DLVEEAVLAE FERLSERGGV LGAMETGYQR
GRIQDESMLY EQRKHDGSLP IVGVNTFTSE ASQEPSGPIE LARGTEEEKR GQLRRLAEFQ
AAHREEAPAA LRRLREAATF GENAFAVLMD TARVCSLGQI TEALFEAGGQ YRRNV
//
