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Database: UniProt
Entry: G3A3P7_9RALS
LinkDB: G3A3P7_9RALS
Original site: G3A3P7_9RALS 
ID   G3A3P7_9RALS            Unreviewed;      1099 AA.
AC   G3A3P7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=RALSY_30252 {ECO:0000313|EMBL:CCA88508.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA88508.1};
RN   [1] {ECO:0000313|EMBL:CCA88508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA88508.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA88508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA88508.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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; FR854088; CCA88508.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3A3P7; -.
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   CDD; cd03678; MM_CoA_mutase_1; 1.
DR   CDD; cd03114; MMAA-like; 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; IPR006159; Acid_CoA_mut_C.
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   NCBIfam; TIGR00640; acid_CoA_mut_C; 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|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          24..162
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   BINDING         37
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         217..222
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         221
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         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
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         308
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         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         355..358
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         588
FT                   /ligand="substrate"
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"
FT   BINDING         1098
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ   SEQUENCE   1099 AA;  121254 MW;  1F1162653B769421 CRC64;
     MTDLSAARAA EPASASEPVP ICNKVRFVTA ASLFDGHDAS INIMRRILQS MGCEVIHLGH
     NRSVDEVVNA ALQEDAQGIA VSSYQGGHVE YFKYMIDALR ARGGEHIQVF GGGGGVIVPA
     EIRELQDYGV ARIYSPEDGQ RMGLAGMIAD MVRRCDIDLS IHAPTTLEPV VAGDRRALAQ
     LITALESGRV DPALRQAVHE RAAATHTPVL GVTGTGGAGK SSLTDELIRR FRLDQHDRLR
     IAVISIDPSR RKSGGALLGD RIRMNAINHP HLFVRSMATR EAGSEISDAL PDAIAACRAG
     GFDLIMVETS GIGQGDAAIV PHVDLSLYVM TPEFGAASQL EKIDMLDFAD LVAINKFDRK
     GAQDAWRDVC KQVQRNREQW HAKPEAMPVF GTQASHFNDD GVTALYHALA DQLAKRGLAL
     GERTLPRPPG TCSTSHDAIV PPARVRYLAE VAEAVRGYHR RAETQSRLAR ERQQLQASRR
     MLEQVGASGD ALAALDTQAA ERDARLGAAE RKLLAMWPDL RRAYAGDEYV VKIRDKEIRT
     RLTHTTLSGT TIRKVVLPPY EDDGEILRWL MRENVPGSFP YTAGVFAFKR RGDDAGEDPT
     RMFAGEGDAF RTNRRFKLVS EGMPAKRLST AFDSVTLYGE DPDPRPDIYG KVGNAGVSIA
     TLDDMKVLYD GFDLTSPDTS VSMTINGPAP TLLAMFMNTA IDQNLDRFRA DNGREPTEGE
     EAKIRAWVLQ NVRGTVQADI LKEDQGQNTC IFSTAFSLKV MGDIQEYFVH HQVRNFYSVS
     ISGYHIAEAG ANPISQLAFT LANGFTYVEA YRARGMHIDD FAPNLSFFFS NGMEPEYSVL
     GRVARRIWAV TMRDKYGANE RSQKLKYHVQ TSGRSLHAQE IAFNDIRTTL QALIAIYDNC
     NSLHTNAYDE AITTPTAESV RRALAIQLII NREWGLTKCE NPNQGSFIID ELTDLVEAAV
     LQEFERIAER GGVLGAMETG YQRGRIQEES MLYEQRKHDG SLPIIGVNTF RDPDAGHAAP
     VPIELARSSE EEKQRQLARL EDFHARHAAE APAMLQRLQR AVIDDQNVFA VLMDAVRVCS
     LGQITHALFE VGGQYRRNM
//
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