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Database: UniProt
Entry: A0A160FG93_9BURK
LinkDB: A0A160FG93_9BURK
Original site: A0A160FG93_9BURK 
ID   A0A160FG93_9BURK        Unreviewed;      1187 AA.
AC   A0A160FG93;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AYM40_00880 {ECO:0000313|EMBL:ANB71069.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB71069.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB71069.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB71069.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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; CP014578; ANB71069.1; -; Genomic_DNA.
DR   RefSeq; WP_063494558.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A160FG93; -.
DR   STRING; 1804984.AYM40_00880; -.
DR   KEGG; buz:AYM40_00880; -.
DR   Proteomes; UP000076852; 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; 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   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; 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; IPR006098; MMCoA_mutase_a_cat.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
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:UP000076852}.
FT   DOMAIN          20..158
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          547..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..569
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:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         274..279
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         278
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         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         317
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         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         369
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         369
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         370
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         416..419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         678
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         713
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         822
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         915
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         950
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         955
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         1067
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
FT   BINDING         1186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02050"
SQ   SEQUENCE   1187 AA;  129723 MW;  E6D94AFF7235AF43 CRC64;
     MTDLSTPQRA GGHKLPAGRR LRFVTAAALF DGHDASINIM RRILQASGVE VIHLGHNRSV
     DEVATAALQE DADGVAVSSY QGGHNEYFRY LVDLLRARGG ERIKVFGGGG GVIVPEEIAE
     LERYGVEKIY SPHDGQRLGL QGMIDDMIAR CAEVARAAAA VRESPVGEWV ADLSACGLPR
     FEPRAESDVE ARADDHANAR DLSGTARQAG GALYASQIDD TAEQPDPAAF TFRRLAQLIS
     AYEAGRVKSA EPEILAVLAE ATEIPVLGIT GTGGAGKSSL TDELIRRFRL DYGDALTIAV
     LAIDPSRRKS GGALLGDRIR MNAIGDWGGG ARVYMRSMAT REASSEITDS LSDVLTLCKA
     AGFDLIIVET SGIGQGNAAI VPFVDESLYV MTPEFGAASQ LEKIDMLDFA SFVAINKFDR
     KGAPDALRDV AKQVQRNRGD FAKAPDAMPV FGTIASRFND DGVTALYQHV AGALRTHGLR
     SGGGRLPRLD DLRFSSGRNA IVPPARVRYL ADVAQTVHAY RERADAQASV ARERWHLTEA
     RRMLGEADAG TGTGTGTGTG TRTGPGASAA TTTGAAAAIH LHTELDTLIA QRTAALGERE
     RRLLEAWPQT VSAYSGDEHI VRIRGREIHT ALTVTTLSGS KVRKVALPKF ADHGEILHWL
     MLDNLPGYFP FTAGVFPFRR ENEDPTRMFA GEGDPFRTNR RFKLLSEGMP AKRLSTAFDS
     VTLYGEEPHE RPDIYGKVGN SGVSVATLDD MKTLYDGFDL CAPETSVSMT INGPAPTILA
     MFFNVAIDQQ IARLNERLQQ EGRKPTGEEL ATARRTALEN VRGTVQADIL KEDQGQNTCI
     FSTEFSLKVM GDIQAYFVDH GVRNFYSVSI SGYHIAEAGA NPISQLAYTL ANGFTYVEAY
     LARGMSIDDF APNLSFFFSN GMDPEYTVLG RVARRIWAIA MRERYGANER SQKLKYHVQT
     SGRSLHAQEI DFNDIRTTLQ ALIAIYDNCN SLHTNAFDEA ITTPTEDSVR RAVAIQLIIN
     REWGLAKNQN PNQGSFVIEE LTDLVEEAVL AEFDRLTERG GVLGAMETGY QRGRIQDESM
     LYEHRKHDGS YPIVGVNTFL SAHPHEAPQP IALARSTDEE KQSQLKRLRD FQARHRNDAP
     AALERLKRAV IDDDNVFAVL MDVVRVCSLG QITHALFEVG GQYRRNM
//
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