ID A0A0U2Z4M2_9BACL Unreviewed; 715 AA.
AC A0A0U2Z4M2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AUC31_02250 {ECO:0000313|EMBL:ALS74148.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS74148.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS74148.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS74148.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013659; ALS74148.1; -; Genomic_DNA.
DR RefSeq; WP_058380856.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2Z4M2; -.
DR STRING; 200991.AUC31_02250; -.
DR KEGG; prt:AUC31_02250; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000067683; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000067683}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 715 AA; 79006 MW; C1ACEA41C92E0B8F CRC64;
MTTPDFTKID VTKLDTAKLG ERDESAFMTN EGIAVKPFYS SKDLNKEQTS YPGFAPNVRG
PYPTMYVSRP WTVRQYAGFS TAEESNAFYR RNLAMGQKGL SVAFDLATHR GYDSDHPRVV
GDVGKAGVAI DSVEDMKILF DGIPLDQMSV SMTMNGAVVP IMAFFIVAAE EQGVSPGQLA
GTIQNDILKE YMVRNTYIYP PAMSMQIIAD IFKYTSDHMP KFNSISISGY HIQEAGATAD
IELAYTLADG LEYVRTGLDA GIGIDQFAPR LSFFWGIGMN YFMEVAKMRA GREIWAKMMK
SFDPQNAKSL ALRTHSQTSG WSLTEQDPFN NVTRTLLEAN AAAMGHTQSL HTNALDEAIA
LPTDFSARIA RNTQLFLQEE TLMNNTIDPW GGSYYVEKLT EELMEKAWTL IEEVEELGGM
AKAIETGLPK MRIEEAAAKK QAQIDSNEET IIGVNRYRLD EEDPIDILNI DNTMVRKKQI
ERLDRMRDTR DQKKVEKALL ELTQAAETGE DNILACAIEA ARHRASLGEI SDAIEKASGR
HKAVIRSVSG VYSSNFSNQE EMQIVKQMTE EFIENEGRRP RILIAKMGQD GHDRGAKVIS
TAFADLGFDV DIGPLFQTPA ETAQQAAEND VHVIGVSSLA AGHMTLVPDL AAELKKVGRE
DILIVVGGVI PAQDYEFLRN NGASAIFGPG TVIPVAAQKV IEEIYARLGY EEEAD
//
