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Database: UniProt
Entry: A0A221SWP8_9DEIO
LinkDB: A0A221SWP8_9DEIO
Original site: A0A221SWP8_9DEIO 
ID   A0A221SWP8_9DEIO        Unreviewed;       140 AA.
AC   A0A221SWP8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:ASN81072.1};
GN   ORFNames=DFI_08720 {ECO:0000313|EMBL:ASN81072.1};
OS   Deinococcus ficus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=317577 {ECO:0000313|EMBL:ASN81072.1, ECO:0000313|Proteomes:UP000259030};
RN   [1] {ECO:0000313|EMBL:ASN81072.1, ECO:0000313|Proteomes:UP000259030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ASN81072.1,
RC   ECO:0000313|Proteomes:UP000259030};
RA   Wu K.-M., Liao T.-L., Liu Y.-M., Young C.-C., Tsai S.-F.;
RT   "The complete genome sequence of Deinococcus ficus isolated from the
RT   rhizosphere of the Ficus religiosa L. in Taiwan.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
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DR   EMBL; CP021081; ASN81072.1; -; Genomic_DNA.
DR   RefSeq; WP_022801691.1; NZ_CP021081.1.
DR   AlphaFoldDB; A0A221SWP8; -.
DR   STRING; 317577.GCA_000419625_02171; -.
DR   KEGG; dfc:DFI_08720; -.
DR   OrthoDB; 9788468at2; -.
DR   Proteomes; UP000259030; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   PANTHER; PTHR48101:SF1; METHYLMALONYL-COA MUTASE, LARGE SUBUNIT; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000259030}.
FT   DOMAIN          5..136
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   140 AA;  15173 MW;  FADC8D365C1C0E61 CRC64;
     MEDRRIRVLI AKPGMDGHDR GAKVVARALR DAGMEVIYTG LRQTADMIVN AALQEDVDAI
     GLSVLSGAHM HYFREVTQLL KDKGASDIIL FGGGIIPDQD LPELEALGVG RVFTPGASTQ
     DAAEYLKEAV QRRWEALGDA
//
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