ICMF_NOCFA
ID ICMF_NOCFA Reviewed; 1071 AA.
AC Q5Z110;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 OrderedLocusNames=NFA_10360 {ECO:0000312|EMBL:BAD55881.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD55881.1; -; Genomic_DNA.
DR RefSeq; WP_011207566.1; NC_006361.1.
DR AlphaFoldDB; Q5Z110; -.
DR SMR; Q5Z110; -.
DR STRING; 247156.NFA_10360; -.
DR EnsemblBacteria; BAD55881; BAD55881; NFA_10360.
DR GeneID; 61131858; -.
DR KEGG; nfa:NFA_10360; -.
DR eggNOG; COG1703; Bacteria.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_2_0_11; -.
DR OMA; LAMFMNT; -.
DR BioCyc; NFAR247156:NFA_RS05250-MON; -.
DR Proteomes; UP000006820; Chromosome.
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..1071
FT /note="Fused isobutyryl-CoA mutase"
FT /id="PRO_0000434126"
FT DOMAIN 12..149
FT /note="B12-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT REGION 153..400
FT /note="GTPase chaperone MeaI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT REGION 401..558
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 25
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 203..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 207
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 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 246
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 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 293
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 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 340..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 601
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 707
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 751
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 800
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 835
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 840
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 952
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
FT BINDING 1070
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1071 AA; 118069 MW; F8D247219504F109 CRC64;
MADSTLHQPA YPVRFVTSAA LFDGHDAAIN IMRRILQSQG AEVIHLGHNR AVHEVVAAAV
EEDVQGVAVS SYQGGHVEYF EYLASALRDA GAGHVRVFGG GGGVIVPEEI ERLARSGVRI
FSPEDGQRLG LPGMINELIQ TCDVDLTGER PAVEAVLAGE RTALARVITC LQQDALPAAD
RDALLAAARD RTVPVLGITG TGGSGKSSLT DELVRRLRTD QQDKLRVAIL AVDPTRRRGG
GALLGDRIRM NSLDGTHVFF RSLATRGGHE LPHDIDAVIA ACKAAGYDLV ILETPGIGQG
DAAIVDHVDV AMYVMTPEFG AASQLEKIDM LDFADVVAIN KFERRGGADA VRDVSRQLLR
NREAFGADPA DMPVFGTSAA TFNDDGVTAL YQHLLELLGA RGLPVDEGVL PRVQTRVSTR
FAQIIPTARV RYLAEIADTV RTYHARTRDQ VAAAQRVQRL ELVAAELPGD AAVADLLARA
RAELDPENAA LLARWPEVAE SYRGPEQVVR VRDREIRTTL RRESLSGSSI PRVALPRFTD
HGELLRFLRS ENLPGHFPFT AGVFPFKRDN EDPARMFAGE GDPFRTNRRF KVLSEHSEAK
RLSTAFDSVT LYGRDPDERP DIYGKVGTSG VSIATVDDMK ALYDGFDLTA PTTSVSMTIN
GPAPTILAFF LNTAIDQALD RFRAAEGREP TADEAADLRA RTLATVRGTV QADILKEDQG
QNTCIFSTEF SLRMMADIQE WFVRNKVRNF YSVSISGYHI AEAGANPISQ LAFTLANGFT
YVEAYLARGM HIDDFAPNLS FFFSNGMDPE YSVIGRVARR IWAIALRDKY GAAERSQKLK
YHVQTSGRSL HAQEMNFNDI RTTLQALIAI YDNCNSLHTN AYDEAVTTPT EDSVRRALAI
QLIINREWGL AMNENPLQGS FIIDELTDLA EEAVLTEFER ISERGGVLGA METGYQRGKI
QDESMLYEHR KHDGSLPIIG VNTFRNPHGE PERTLELARA TEREKQSQLD RVREFQRRHR
TQAQAALARL EEVARTDENI FEVLMDAARV CSLQQVTETF FTVGGQYRRN V
