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Database: UniProt
Entry: A0A0A0JQH5_9MICO
LinkDB: A0A0A0JQH5_9MICO
Original site: A0A0A0JQH5_9MICO 
ID   A0A0A0JQH5_9MICO        Unreviewed;      1080 AA.
AC   A0A0A0JQH5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=N803_11100 {ECO:0000313|EMBL:KGN38287.1};
OS   Knoellia subterranea KCTC 19937.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN38287.1, ECO:0000313|Proteomes:UP000030011};
RN   [1] {ECO:0000313|EMBL:KGN38287.1, ECO:0000313|Proteomes:UP000030011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN38287.1,
RC   ECO:0000313|Proteomes:UP000030011};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia subterranea.";
RL   Submitted (AUG-2013) 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: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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:KGN38287.1}.
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DR   EMBL; AVPK01000003; KGN38287.1; -; Genomic_DNA.
DR   RefSeq; WP_035903873.1; NZ_AVPK01000003.1.
DR   AlphaFoldDB; A0A0A0JQH5; -.
DR   STRING; 1385521.N803_11100; -.
DR   eggNOG; COG1703; Bacteria.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000030011; 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|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:UP000030011}.
FT   DOMAIN          14..151
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          404..565
FT                   /note="Linker"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         27
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         206..211
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         210
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         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         236
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         249
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         252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         296
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         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         343..346
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         573
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         608
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         714
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         758
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         807
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         842
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         847
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         959
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         1079
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ   SEQUENCE   1080 AA;  118384 MW;  9C2383C9A3B60639 CRC64;
     MTQTSPELHV PTNPVRIVTA SSLFDGHDAS INIMRRIMQS QGAEVIHLGH NRSVQEVVDA
     AIEEDVQGVA VSSYQGGHVE YFEYLVQLLR EAGAGHVKVV GGGGGVIVAD EIARLREAGV
     TIFSPEDGQR LGLVGMINTV IEDCDTDLYA VRSASVAGVL SGDRAAVARA ITGAETHKLS
     DDDRAELARA AEARHVPVLG ITGTGGSGKS SLTDELVRRL RVDQQDKLRV AVVAVDPTRR
     KGGGALLGDR IRMNSLDGDR IFFRSLATRG GREVPEALED VITILKAAAY DLIVIETPGI
     GQGDAAIVPF ADVSMYVMTP EFGAQSQLEK IDMLDFADLV AINKFERRGA MDALRDVGRQ
     LVRNRNAFGK KPEDMPVFGT SAATFNDDGV TALYQELRRL LSEKGLEFSE GVLPPVSVRH
     SSVLRQIVPA ARVRYLSEIA DTVRGYHSQT EAYAAHARRV QRLEFVDDEL AAAGHEDHAV
     DALLVEARKA LPTEVGEAIE NWPATVEAYA GDEQVVRIRD KELHTSLVKE SLSGNKIRRV
     SVPSFADHGD LVSFLRRENL PGFFPFTAGV FPFKRDNEDP ARMFAGEGDP FRTNRRFKLL
     SEGQPATRLS TAFDSVTLYG RDPDPRPDIY GKVGTSGVSI ATLDDMKALY DGFDLTSPST
     SVSMTINGPA PTILAFFLNT VIDGELAKFS EREGREPNAE EAAGIRAHAL ASVRGTVQAD
     ILKEDQGQNT CLFSTEFSLR MMADIQEWFI EQQVRNFYSV SISGYHIAEA GANPISQLAF
     TLANGFTYVE AYLARGMDIN DFAPNLSFFF SNGMDPEYSV IGRVARRIWA VAMREKYGAN
     ERSQKLKYHV QTSGRSLHAQ EMDFNDIRTT LQALIAIYDN ANSLHTNAFD EAVTTPGPDS
     VRRALAIQMI INREWGLAMN ENPLQGSYVI DELTDMVEAA VLAEFDRISE RGGVLGAMET
     GYQRGKIQDE SMLYEHRKHD GSLPIIGVNT FRKPDAEGGT PQHVELARAS ESEKESQLAR
     VRAYREAHSV EAEEELGRLR EAAMSGDNVF AVLMDAARVC TLQQVTDAFF EVGGQYRRNV
//
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