ID A0A0S8EEH2_9CHLR Unreviewed; 135 AA.
AC A0A0S8EEH2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:KPK46482.1};
GN ORFNames=AMJ77_05980 {ECO:0000313|EMBL:KPK46482.1};
OS Dehalococcoidia bacterium SM23_28_2.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703396 {ECO:0000313|EMBL:KPK46482.1, ECO:0000313|Proteomes:UP000054036};
RN [1] {ECO:0000313|EMBL:KPK46482.1, ECO:0000313|Proteomes:UP000054036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_2 {ECO:0000313|EMBL:KPK46482.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK46482.1}.
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DR EMBL; LJUA01000073; KPK46482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EEH2; -.
DR STRING; 1703396.AMJ77_05980; -.
DR PATRIC; fig|1703396.3.peg.756; -.
DR Proteomes; UP000054036; 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 5..133
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 135 AA; 14416 MW; 94D00330D12A0A21 CRC64;
MTKGKIKVLI AKTGLDGHDR GAKVVARALR DAGLEVVYTG LRQTPEMVAE AALQEDVDLV
GLSILSGAHM ELFPRVAEEM RKRGLDDVAL LGGGIIPQED IPALQKAGFR AIFGPGASTD
EIVAWVRANI TSRVQ
//