ID A0A0S7YSD4_9DELT Unreviewed; 1087 AA.
AC A0A0S7YSD4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AMJ54_07320 {ECO:0000313|EMBL:KPJ77599.1};
OS Deltaproteobacteria bacterium SG8_13.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ77599.1, ECO:0000313|Proteomes:UP000051346};
RN [1] {ECO:0000313|EMBL:KPJ77599.1, ECO:0000313|Proteomes:UP000051346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ77599.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ77599.1}.
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DR EMBL; LJNK01000020; KPJ77599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YSD4; -.
DR STRING; 1703398.AMJ54_07320; -.
DR PATRIC; fig|1703398.3.peg.2109; -.
DR Proteomes; UP000051346; 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}.
FT DOMAIN 13..143
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT COILED 483..518
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 26
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 211..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 215
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 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 253
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 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 301
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 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 348..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 720
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 764
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 813
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 848
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 853
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 965
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT BINDING 1086
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ SEQUENCE 1087 AA; 121542 MW; 414E809BEB90FBBF CRC64;
MSDKAEIYKP RHPIRVVTAT SLFDGHDAAI NIMRRILQAT GVEVIHLGHN RAVSEIVDAA
IEEDAQGIAV SSYQGGHIEY FKYMVDLLKE RKAAHIKVFG GGGGVIVPAE ISELEAYGVA
KIYSPEDGAR WGLQGMINHM VRQLDFPTVN ETDFDFKALQ PDNKLLIANL ITAMEQAKAE
QNGHLAELRS RLKKKTGSRR VPVIGITGTG GAGKSSLTDE LIIRLLHDLP EIHLAVLSCD
PSRRKTGGAL LGDRIRMNGI ANPRVYMRSL ATRRSQTEIP DSLVEAVSVA KAAGFDLIIV
ETAGIGQGDS MIVDMVDVSM YVMTSEFGAA SQLEKIDMLD FADIVAVNKY EKRGGEDAVR
DVRKQVQRNR NAFESAPEEM PVFGTIASRF NDDGVTALYH SLMELVAEKT GTVYRSTLAR
PETKTSTSKA IIIPPERTRY LAEIAEAVRG YHAETAEQAQ AIRGAWHIEE TARQIGDDQA
ELAARLQAET EKARQQINEQ TRQVLKQWEE IKEIYEADEL AYNVRNREIR TPLFVESLSH
LRIPKIMLPR FSDPAEIYRW MREENVAGRF PFTAGVFPLR RVDEEPTRMF AGEGDPARTN
RRFKLLSADY EAKRLSTAFD SVTLYGYDPD IRPDIYGKVG TSGVSICTLD DVRVLYSGFE
LCAPNTSVSM TINGPAPIIL AMFLNAAIDQ QVDRFSTENG HGPAPEHYAR IRSEVLSNVR
GTVQADILKE DQGQNTCIFS IDFALKMMGD IQQYFIGNNV RNFYSVSISG YHIAEAGANP
ISQLAFTLAN GFTYVEYYLS RGMPLDSFAP NLSFFFSNGM DPEYTVIGRV ARRIWALAMR
QKYNGSARSQ MLKYHIQTSG RSLHSQDIQF NDIRTTLQAL IAIYDNCNSL HTNAFDEAIT
TPSTESVRRA LAIQMIINRE WGLTKNENPQ QGSFIVEELT RLVEEAVLME FDRITERGGV
LGAMETGYQR SKIQEESIYY EMLKHTGEMP IIGVNTFRDP HTDQELLFDS VDLARATEEE
KQSQLKRLAD FQQRNSDKSA QALARLQQVA LSGENIFAEL MNTVRVCSLG QITQALYDVG
GKYRRNM
//
