ID   D0TQU8_9BACE            Unreviewed;       715 AA.
AC   D0TQU8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=HMPREF0102_01948 {ECO:0000313|EMBL:EEZ04779.1};
OS   Bacteroides sp. 2_1_22.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ04779.1, ECO:0000313|Proteomes:UP000005775};
RN   [1] {ECO:0000313|EMBL:EEZ04779.1, ECO:0000313|Proteomes:UP000005775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ04779.1,
RC   ECO:0000313|Proteomes:UP000005775};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL   Submitted (JUL-2009) 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; GG705174; EEZ04779.1; -; Genomic_DNA.
DR   RefSeq; WP_008641116.1; NZ_GG705174.1.
DR   AlphaFoldDB; D0TQU8; -.
DR   GeneID; 69481486; -.
DR   HOGENOM; CLU_009523_3_1_10; -.
DR   Proteomes; UP000005775; 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: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.
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, ECO:0000313|EMBL:EEZ04779.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          586..715
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   715 AA;  78803 MW;  E75E08BB2700A823 CRC64;
     MRKDFKNIDI YAAFQPANGA EWQKANGISA DWKTPEHIEV KPVYTKEDLE GMEHLGYAAG
     LPPYLRGPYS VMYTLRPWTI RQYAGFSTAE ESNAFYRRNL ASGQKGLSVA FDLATHRGYD
     PDHERVVGDV GKAGVSICSL ENMKVLFDGI PLNKMSVSMT MNGAVLPIMA FYINAGLEQG
     AKLEEMAGTI QNDILKEFMV RNTYIYPPAF SMKIISDIFE YTSQKMPKFN SISISGYHMQ
     EAGATADIEL AYTLADGLEY LRAGTAAGID IDAFAPRLSF FWAIGTNHFM EIAKMRAARM
     LWAKIVKQFN PKNPKSLALR THSQTSGWSL TEQDPFNNVG RTCIEAMAAA LGHTQSLHTN
     ALDEAIALPT DFSARIARNT QIYIQEETYI CKNVDPWGGS YYVESLTNEL AHKAWEHIQE
     IEKLGGMAKA IETGIPKMRI EEAAARTQAR IDSGQQTIVG VNKYRLEKEA PIDILEIDNT
     AVRLEQIENL KRLKEGRNQA EVDKALAAIT ECVKTGKGNL LELAVEAARV RATLGEISYA
     CEQVVGRYKA IIRTISGVYS SESKNDSDFK RACELAEKFA KKEGRQPRIM VAKMGQDGHD
     RGAKVVATGY ADCGFDVDMG PLFQTPAEAA REAVENDVHV VGVSSLAAGH KTLVPQIIEE
     LKKLGREDIV VIAGGVIPAQ DYDFLYKAGV AAIFGPGTPV AKAACQILEI LMDEE
//