ID A0A229FS22_9BURK Unreviewed; 722 AA.
AC A0A229FS22;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AOC33_05740 {ECO:0000313|EMBL:OXL14827.1};
OS Polynucleobacter cosmopolitanus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=351345 {ECO:0000313|EMBL:OXL14827.1, ECO:0000313|Proteomes:UP000215188};
RN [1] {ECO:0000313|EMBL:OXL14827.1, ECO:0000313|Proteomes:UP000215188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoIso2 {ECO:0000313|EMBL:OXL14827.1,
RC ECO:0000313|Proteomes:UP000215188};
RA Hahn M.W.;
RT "Reclassification of a Polynucleobacter cosmopolitanus strain isolated from
RT tropical Lake Victoria as Polynucleobacter victoriensis comb. nov.";
RL Submitted (JUN-2017) 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}.
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:OXL14827.1}.
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DR EMBL; NJGG01000002; OXL14827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229FS22; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000215188; Unassembled WGS sequence.
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:InterPro.
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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 592..722
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 722 AA; 78848 MW; 0BC87DA08839CCE2 CRC64;
MSKTTKSPWP EFSNPSLEAW EKSAAKSAPN GNVDALGWDT PDDIKLKALY TAADTEGLPF
ANTLPGFEPF VRGPQATMYS VRPWTIRQYA GFSTAEESNA FYRKALAAGG QGVSVAFDLA
THRGYDSDHP RVTGDVGKAG VAIDSVEDMK ILFNQIPLDK VSVSMTMNGA VLPILAGYVV
AAEEQGVSQD QLSGTIQNDI LKEFMVRNTY IYPPEPSMRI IGDIIEYTSQ KMPKFNSISI
SGYHIQEAGA NQALELAFTI ADGKEYVKTA LSKGLDVDGF AGRLSFFFAI GMNFYLEVAK
LRAARLLWWR VMKEFNPKNP KSLMLRTHCQ TSGWSLTEQD PYNNVVRTTI EAMAAVFGGT
QSLHTNSFDE AIALPTEFSS RIARNTQLII QEETHITNVI DPWAGSYMME KLTQDMADKA
WDIIQEVEGM GGMTKAVESG WAKLKIEAAA AEKQACIDSG KDVIVGVNKY KLGKEDPIDI
LDIDNNKVRD SQIARLKDVR AKRDSQKVQA ALDALTAAAE NNTGNLLALA IDAIRLRATV
GEVSDALEKV YGRHRADTQK VTGVYAAAYD SAEGWEKLKT EIAEFAKDQG RHPRVMIAKL
GQDGHDRGAK VVATAFADLG FDVDMGPLFQ TPEECARQAI ENDVHAVGIS TLAAGHKTLV
PAIIQELKKQ GADDIIVFVG GVIPRQDYEF LYEAGVKGIY GPGTPIPASA KDVLEQIRLA
QK
//
