ID A0A1K1M5T2_9BACT Unreviewed; 721 AA.
AC A0A1K1M5T2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN02910409_0748 {ECO:0000313|EMBL:SFW18439.1};
OS Prevotellaceae bacterium HUN156.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1520830 {ECO:0000313|EMBL:SFW18439.1, ECO:0000313|Proteomes:UP000182805};
RN [1] {ECO:0000313|EMBL:SFW18439.1, ECO:0000313|Proteomes:UP000182805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUN156 {ECO:0000313|EMBL:SFW18439.1,
RC ECO:0000313|Proteomes:UP000182805};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FPIT01000004; SFW18439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1M5T2; -.
DR STRING; 1520830.SAMN02910409_0748; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000182805; 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:UP000182805}.
FT DOMAIN 593..721
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 721 AA; 80024 MW; 535218DA420EF0D1 CRC64;
MARKNFNNID IYAGIQKKNG QQWQKENGIS ANWRTPEQID IQPVYTKEDL EGMEHLDFTA
GIPPYLRGPY SMMYPFRPWT IRQYAGFSTA EESNAFYRRN LASGQKGLSV AFDLPTHRGY
DPDNARVVGD VGKAGVSICN EENMKVLFSG IPLNKMSVSM TMNGAVLPIL AFYIVAGLEQ
GAQLEEMAGT IQNDILKEFM VRNTYIYPPA FSMKIIADIF EYTSQKMPKF NSISISGYHM
QEAGATADIE LAYTLADGMD YLRTGVNAGI DVDAFAPRLS FFWAIGMNHF MEIAKMRAGR
LLWAKIVKSF GAKNPKSLAL RTHSQTSGWS LTEQDPFNNV GRTCIEAMAA VLGHTQSLHT
NALDEAIALP TDFSARIARN TQIYIQNETK VCKQIDPWAG SYYVETLTNE LVHKAWEHIQ
EIEKLGGMAK AIETGLPKMR IEEAAARTQA RIDSGTQTIV GINKYRLEHE DPIDILEVDN
TAVRKQQEEN LKEVRSKRDE AACQAALKAI TDCVRDFKEG RKSENNLLDL AVKAAQLRCT
LGEISDACEE IVGRYKAVIR TISGVYSSES KNDANFELAK QMTDKFAERE GRRPRIFIAK
MGQDGHDRGA KVVATGYADC GFDVDMGPLF QTPAEAAREA VENDVHIVGA SSLAAGHKTL
IPQLIEELKK LGREDIMVTA GGVIPAQDYD FLYKAGVACI FGPGTPIPYS AVEMMKILLD
E
//
