ICMF_PARXL
ID ICMF_PARXL Reviewed; 1272 AA.
AC Q146L7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Fused isobutyryl-CoA mutase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
DE Includes:
DE RecName: Full=Isobutyryl-CoA mutase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
DE Short=ICM {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
DE EC=5.4.99.13 {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:19864421};
DE Includes:
DE RecName: Full=P-loop GTPase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q5KUG0, ECO:0000255|HAMAP-Rule:MF_02050};
DE AltName: Full=G-protein chaperone {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
GN Name=icmF {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:19864421};
GN ORFNames=Bxe_A4277 {ECO:0000312|EMBL:ABE28722.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=19864421; DOI=10.1074/jbc.m109.062182;
RA Cracan V., Padovani D., Banerjee R.;
RT "IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and
RT its G-protein chaperone.";
RL J. Biol. Chem. 285:655-666(2010).
CC -!- FUNCTION: Catalyzes the reversible interconversion of isobutyryl-CoA
CC and n-butyryl-CoA, using radical chemistry (PubMed:19864421). Also
CC exhibits GTPase activity, associated with its G-protein domain (MeaI)
CC that functions as a chaperone that assists cofactor delivery and proper
CC holo-enzyme assembly (By similarity). Does not exhibit methylmalonyl-
CC CoA mutase (MCM) activity (PubMed:19864421).
CC {ECO:0000250|UniProtKB:Q1LRY0, ECO:0000269|PubMed:19864421}.
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:0000255|HAMAP-Rule:MF_02050,
CC ECO:0000269|PubMed:19864421};
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:0000255|HAMAP-
CC Rule:MF_02050};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02050};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02050};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_02050, ECO:0000269|PubMed:19864421}.
CC -!- SIMILARITY: Belongs to the IcmF family. {ECO:0000255|HAMAP-
CC Rule:MF_02050, ECO:0000305}.
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DR EMBL; CP000270; ABE28722.1; -; Genomic_DNA.
DR RefSeq; WP_011486567.1; NZ_CP008760.1.
DR AlphaFoldDB; Q146L7; -.
DR SMR; Q146L7; -.
DR STRING; 266265.Bxe_A4277; -.
DR EnsemblBacteria; ABE28722; ABE28722; Bxe_A4277.
DR KEGG; bxb:DR64_1955; -.
DR KEGG; bxe:Bxe_A4277; -.
DR PATRIC; fig|266265.5.peg.194; -.
DR eggNOG; COG1703; Bacteria.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR OMA; LAMFMNT; -.
DR OrthoDB; 154460at2; -.
DR Proteomes; UP000001817; 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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cobalamin; Cobalt; GTP-binding; Hydrolase; Isomerase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1272
FT /note="Fused isobutyryl-CoA mutase"
FT /id="PRO_0000434128"
FT DOMAIN 20..158
FT /note="B12-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT REGION 163..536
FT /note="GTPase chaperone MeaI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT REGION 193..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..758
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT REGION 614..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Polar residues"
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:0000255|HAMAP-Rule:MF_02050"
FT BINDING 334..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 476..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 801
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 907
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 951
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1000
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1035
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1040
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1272 AA; 137407 MW; 317A80BC28FBC3B7 CRC64;
MTDLSTPQRA GSHKLPAGRR LRFVTAAALF DGHDASINIM RRILQASGVE VIHLGHNRSV
DEVATAALHE DADGVAVSSY QGGHNEYFRY LVDLLRARGG ERIKVFGGGG GVIVPEEIAG
LERYGVEKIY SPQDGQRLGL QGMIDDMIAR CAEGARAAAA TGESQVGAWA AEFSEHGLPR
FDSRDDVGVD RQGAVARNPS SEASRVAAAG RGDHLDRGVR AASTADTADT ANTANTANTA
NTGSVADAAD AADAADAADA ADAASTASTA STASTASTAS TAGIPDPASL VFRRLAQLIS
AFETAAIDVN TRDKLSALAE VTAIPLLGIT GTGGAGKSSL TDELIRRFRL DYGDALTIAV
LAIDPSRRKS GGALLGDRIR MNAIGDWGGG ARVYMRSMAT REASSEISDS LPDALMLCKA
AGFDLIVVET SGIGQGNAAI VPFVDESLYV MTPEFGAASQ LEKIDMLDFA SFVAINKFDR
KGARDALRDV AKQVQRNRAD FAKSPEAMPV FGTIASRFND DGVTALYRHV AEALRKHGLR
SGGGRLAAPE DLRFSSGRNA IVPPARVRYL ADIAQTIHAY RERADAQARL ARERWQLIEA
RRMLVETGEA ARSTVATSAS PGASASSKAN ACTSTSSKAN ASPGANTTAN SNASATSGTA
TPTDALNPTL SQLDTLITQR TASLGERERI LLDTWPEIVA AYSGTEHIVR VRDREIRTAL
TVATLSGSEV RKVSLPKFVD HGEILRWLML DNLPGYFPFT AGVFPFRREN EDPTRMFAGE
GDPQRTNRRF KLLSEGMPAK RLSTAFDSVT LYGEEPHERP DIYGKVGNSG VSVATLDDMK
TLYDGFDLCA PETSVSMTIN GPAPTILAMF FNVAIDQQIA RTTQRQGRPL TEDELAATRR
TALENVRGTV QADILKEDQG QNTCIFSTEF SLKVMGDIQA YFVEHGVRNF YSVSISGYHI
AEAGANPISQ LAYTLANGFT YVEAYLARGM SIDDFAPNLS FFFSNGMDPE YTVLGRVARR
IWAVAMRERY GANERSQKLK YHVQTSGRSL HAQEIDFNDI RTTLQALIAI YDNCNSLHTN
AFDEAITTPT EESVRRAVAI QLIINREWGL AKNQNPNQGS FVIEELTDLV EEAVLAEFDR
LTERGGVLGA METGYQRGRI QDESMLYEHR KHDGSYPIVG VNTFLSAHPH EAPQPIALAR
STDDEKQSQL QRLRAFQAQH RDAAPAALER LKRAVIDDEN VFAVLMDVVR VCSLGQITHA
LFEVGGQYRR NM
