ID A0A4U8VBJ9_9BURK Unreviewed; 1097 AA.
AC A0A4U8VBJ9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=MW7_014175 {ECO:0000313|EMBL:TMS57102.1};
OS Burkholderiaceae bacterium PBA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae.
OX NCBI_TaxID=795666 {ECO:0000313|EMBL:TMS57102.1, ECO:0000313|Proteomes:UP000004277};
RN [1] {ECO:0000313|EMBL:TMS57102.1, ECO:0000313|Proteomes:UP000004277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBA {ECO:0000313|EMBL:TMS57102.1,
RC ECO:0000313|Proteomes:UP000004277};
RA Gan H.M.;
RT "Revised genome assembly of Burkholderiaceae (previously Ralstonia) sp.
RT PBA.";
RL Submitted (MAY-2019) 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:TMS57102.1}.
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DR EMBL; AKCV02000025; TMS57102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8VBJ9; -.
DR STRING; 795666.MW7_0203; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000004277; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000004277}.
FT DOMAIN 27..165
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT BINDING 40
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 219..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 223
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 262
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 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 310
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 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 357..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 627
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 777
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 826
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 861
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 866
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 978
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1097 AA; 119242 MW; 2D823F1ABCD9623D CRC64;
MTDLSDARLR GGYADGDSNR DRAARGPLRF VTAAALFDGH DASINIIRRV LQAAGCEVIH
LGHDRSVEVV VTAALQEDAD AIAVSSYQGG HVEYFRYMVE QLHARGGAHI QVFGGGGGVI
VPDEIALLHA AGVTRLYSAQ DGQALGLRGM VDDMIARCYA AARPAPVEVG DVLAGCDVAL
ARYLSQCAGG RVLAETRAAV QAAAMTRRVP VLGITGTGGA GKSSLTDELI RRFRLDDAET
LRIAILCVDP SRRKSGGALL GDRIRMNAIH HPRIFMHSLA TRDSVAEVPA HLPDAIDACK
ASGFDLIVVE TSGIGQGDAA IVPLADVSLY VMTPEFGAAS QLEKIDMLDF ADFVVINKFD
RRGAADAWRD VAKQVQRNRE CWNVAPEDMP VYGTQASRFN DSGVTALYHA LRTALVPHGL
PPSGARLARP AGKTTALGQA IVPPARSRYL SEVADTVRRY HARVSRQSAV ARECQQLDAA
QRLLAAEGGA PDDPALQRLA ELAAKRSAQL DEDAQALLTA WPDLQARYAA DQLVTQVRGH
ERSSPLVTHT LSGTPIRKVL LPAYHDTGDI LCWLMRENVP GAFPYTAGVF PLRRDKEEPT
RMFAGEGDAF RTNRRFHLLS SGMPAKRLST AFDSVTLYGE DPAERPDIYG KIGNAGVSIA
TLDDMQALYA GFDLCDPDTS VSMTINGPAP TVLAMFLQTA IRQRVERFSA EQGRVPDVAE
RAQLEAETLR IVRGTVQADI LKEDQGQNTC IFSTDFSLKM MGDIQAYFIE HEVRNFYSVS
ISGYHIAEAG ANPISQLAFT LANGLTYVEA YLARGMHIDA FAPNLSFFFS NGMDPEYSVL
GRVARRIWAI AMRDRYGANA RSQKLKYHVQ TSGRSLHAQE IAFNDIRTTL QALIALYDNC
NSLHTNAYDE AVTTPSAESV RRALAIQLII NREWGPSRCE NPNQGSFLIE SLTDLVEEAV
LREFDRLTER GGVLGAMETG YQRGRIQDES MLYEQRKHDG TLPIVGVNTF LAPGAEAAPT
PELARSTEAE KHSQLARLAA FHARHAGAAP AMLTRLQQAV LEDANVFAVL MDAVQVCSLG
QITHALFEVG GQYRRTM
//
