ID A0A1Q3SJU4_9CHLR Unreviewed; 161 AA.
AC A0A1Q3SJU4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:OJV89706.1};
GN ORFNames=BGO39_37015 {ECO:0000313|EMBL:OJV89706.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV89706.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJV89706.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJV89706.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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 -!- 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:OJV89706.1}.
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DR EMBL; MKTJ01000077; OJV89706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3SJU4; -.
DR STRING; 1895928.BGO39_37015; -.
DR Proteomes; UP000186384; Unassembled WGS sequence.
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}.
FT DOMAIN 10..138
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 139..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 17244 MW; 19EF679EFD477506 CRC64;
MVSENFRERP IRVLIAKPGL DGHDRGAKVV TRGLRDAGME VIYTGLHQTP EMIVEAALQE
DVDAIGLSIL SGAHNVLFPR IMKLLKENQM EDVLVFAGGI IPPEEEPQIR ALGIGAVFGP
GTTIEDTANF IRQNVRPDAG LASGETSGGS ETWVDAGDKG Q
//
