ID A0A1H6T259_9DEIO Unreviewed; 711 AA.
AC A0A1H6T259;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN04488058_101409 {ECO:0000313|EMBL:SEI71187.1};
OS Deinococcus reticulitermitis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=856736 {ECO:0000313|EMBL:SEI71187.1, ECO:0000313|Proteomes:UP000199223};
RN [1] {ECO:0000313|Proteomes:UP000199223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNZA01000001; SEI71187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6T259; -.
DR STRING; 856736.SAMN04488058_101409; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000199223; 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}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 76487 MW; 4611FDF7A1CFF61C CRC64;
MADLSAWKAL ASKDLKGGDP ESLNRQTPEG LTLKALYTRD DLPPGGAADT LPGLPPFTRG
PRATMYAARP WTIRQYAGFS TAEESNAFYR RNLAAGQKGL SVAFDLATHR GYDSDHPRVV
GDVGKAGVAI DSVEDMKILF DGIPLREMSV SMTMNGAVLP ILAGYIVAGL EQGAKLDELS
GTIQNDILKE FMVRNTYIYP PEPSMRIIAD IIEYTAQNMP RFNSISISGY HIQEAGANAA
LELAYTLADG REYVQAALNK GLSIDDFAGR LSFFFGIGMN FYTEVAKLRA ARLLWSEIVE
EFGPQKPMSK ALRTHCQTSG WSLTEQDAYN NVVRTTIEAM AAVFGGTQSL HTNAFDEAIG
LPTDFSARIA RNTQLVLQEE TGITDVIDPW GGSYLMERLT ADLADKAREL MKEVEGLGGM
AKAIESGIPK LRIEESAARK QARIDRGEDV IVGVNKYRPT QETPIDVLDI DNAAVRESQL
ARLKKVRAER DPEAVTRALD ALTECARSGA GNLLALSVEA MRARATLGEV SDALEKVWGR
HAAEIKTLSG VYAAGYEGDE GFAALQGEIE AFAEKEGRRP RMLVVKMGQD GHDRGAKVIA
TGFADLGFDV DVGPLFQTPE EAARQAIEND VHVVGVSSQA AGHKTLVPQL IAALRAEGAG
DIKVVVGGVI PQQDYPALRE AGAAGIFGPG TPILHSAREV LGILRGAPAT A
//
