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Database: UniProt
Entry: A0A140L0A0_9CLOT
LinkDB: A0A140L0A0_9CLOT
Original site: A0A140L0A0_9CLOT 
ID   A0A140L0A0_9CLOT        Unreviewed;       132 AA.
AC   A0A140L0A0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:KXG73975.1};
DE            EC=5.4.99.2 {ECO:0000313|EMBL:KXG73975.1};
GN   Name=scpA_3 {ECO:0000313|EMBL:KXG73975.1};
GN   ORFNames=AN619_27320 {ECO:0000313|EMBL:KXG73975.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG73975.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG73975.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG73975.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT   isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL   Submitted (DEC-2015) 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:KXG73975.1}.
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DR   EMBL; LOEE01000070; KXG73975.1; -; Genomic_DNA.
DR   RefSeq; WP_068557825.1; NZ_LOEE01000070.1.
DR   AlphaFoldDB; A0A140L0A0; -.
DR   STRING; 520762.AN619_27320; -.
DR   PATRIC; fig|520762.4.peg.3015; -.
DR   OrthoDB; 9788468at2; -.
DR   Proteomes; UP000070456; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
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   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, ECO:0000313|EMBL:KXG73975.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070456}.
FT   DOMAIN          4..132
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   132 AA;  14220 MW;  557A1C012E1DC564 CRC64;
     MDRPIRVLVA KPGLDGHDRG AKVIARALRD AGMEVIYTGL RQTPEQIVNA AIQEDVDVVA
     MSILSGAHNT LLPKVVELLK AENVDDVLVI GGGVIPDDDI PFLKEKGIAE IFTPGTPTSV
     TIDFIRANVK RK
//
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