ID A0A2C1KQ61_9BACI Unreviewed; 717 AA.
AC A0A2C1KQ61;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=COD11_07070 {ECO:0000313|EMBL:PGT87674.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT87674.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT87674.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT87674.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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:PGT87674.1}.
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DR EMBL; NUMC01000028; PGT87674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1KQ61; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000222674; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000222674}.
FT DOMAIN 581..713
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 717 AA; 80240 MW; C89C31DCD3BE579F CRC64;
MKRLSISDAP LVKTKTNIQQ DTNSSPFMTN EQIEVKNVYR KDDLENCRHL GTFPGVEPFV
RGPYATMYVN RPWTIRQYAG FSTAEESNAF YRRNLQMGQK GLSVAFDLAT HRGYDSDHPR
VVGDVGKAGV AIDSILDMKI LFDQIPLDEM SVSMTMNGAV LPIMAFYIVT AEEQGVSKEK
LTGTIQNDIL KEYMVRNTYI YPPEMSMKII GDIFEYTAKN MPKFNSISIS GYHMQEAGAP
ADLELAYTLA DGLEYIRTGL KAGLTIDQFA PRLSFFWAIG MNYFMEVAKM RAARYLWSSI
VKDFKPQNPK SLALRTHSQT SGWSLTEQDP FNNVVRTCIE AHAAAMGHTQ SLHTNALDEA
IALPTDFSAR IARNTQLYLQ NETGICDVID PWGGSYYVES LTHSLIERAK KHIDEIEELG
GMTKAIETGL PKMKIEEAAA RRQAKIDSGR EVIIGVNKFR LDHEDPIDIL SINNTEVRKK
QIERIRQLKE NRNEDEVNHA LHLLTKAAAS GEGNLLELAV EAARKRATLG EISFAIEKVS
KRHQAMIRSI SGVYSSEYSN DEEIKKVRER TDQFYELEGR RPRILIAKMG QDGHDRGAKV
IATAFADLGF DVDIGPLFQT PEETAKQAVE NDVHVVGMSS LAAGHKTLLP QLISELKKLG
REDIVVIIGG VIPFQDYEEL KEKGAAEIFG PGTVIPVAAE KVLKKVFDVL GYEELQE
//
