ID A0A0E3V0J9_9BURK Unreviewed; 731 AA.
AC A0A0E3V0J9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=CL55_00010160 {ECO:0000313|EMBL:AKD25349.1};
OS Polynucleobacter duraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1835254 {ECO:0000313|EMBL:AKD25349.1, ECO:0000313|Proteomes:UP000061135};
RN [1] {ECO:0000313|EMBL:AKD25349.1, ECO:0000313|Proteomes:UP000061135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoK4 {ECO:0000313|EMBL:AKD25349.1,
RC ECO:0000313|Proteomes:UP000061135};
RA Hahn M.W.;
RT "Genome of Polynucleobacter strain MWH-MoK4.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; CP007501; AKD25349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3V0J9; -.
DR STRING; 1835254.CL55_00010160; -.
DR KEGG; pdq:CL55_00010160; -.
DR PATRIC; fig|576611.7.peg.1032; -.
DR HOGENOM; CLU_009523_3_1_4; -.
DR Proteomes; UP000061135; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 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; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 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 PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AKD25349.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 599..731
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 79988 MW; 34EEEB5FD86A14AF CRC64;
MSTSEKKSVL NSSNTWPNVP DCDLDAWKKS AQKSAPNGDV DKLGWQTPDG IHLKALYTAQ
DTEGLQYTHS LPGFEPFVRG PQATMYSVRP WTIRQYAGFS TAEESNAFYR KALDAGGQGV
SVAFDLATHR GYDSDHPRVT GDVGKAGVAI DSVEDMKILF DGIPLDKVSV SMTMNGAVLP
VLAGYIVAGE EQGVKQELLS GTIQNDILKE FMVRNTYIYP PEPSIRIIGD IIEYTAKHMP
KFNSISISGY HMQEAGANQV LELAFTLADG KEYVKTALAK GLDVDGFAGR LSFFFAIGMN
FYLEVAKLRA ARLLWWRIMK SFEPKNPKSL MLRTHCQTSG WSLTEQDPYN NVVRTTVEAM
AAVFGGTQSL HTNSFDEAIA LPSEFSSRIA RNTQLILQEE THITSVIDPW AGSYMMENLT
QEMADKAWEI VQEVDAMGGM TKAVESGWAK LKIEAAAAEK QAKIDSGSDV IVGVNKYKLG
KEDLVDVLMI DNDKVRESQV ARLKEIKAKR DSKKVEAALE ALTKAAEENT GNLLELAVQA
IRLRATVGEV SDALEKVYGR HRADTQKVTG VYAAAYDSAE GWDKLKVEIA DFAKDFGRRP
RVMIAKLGQD GHDRGAKVVA TAFADLGFDV DIGPLFQTPE ECARQAIEND VHALGVSTLA
AGHKTLVPAI IAELKKQGAD DIIVFVGGVI PRQDYEFLYE AGVKGIYGPG TPIPASAKDV
LEQIRKSVKP D
//
