ID A0A0P1IB83_9RHOB Unreviewed; 708 AA.
AC A0A0P1IB83;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=scpA_1 {ECO:0000313|EMBL:CUJ85927.1};
GN ORFNames=RUE5091_00405 {ECO:0000313|EMBL:CUJ85927.1};
OS Ruegeria denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUJ85927.1, ECO:0000313|Proteomes:UP000051260};
RN [1] {ECO:0000313|EMBL:CUJ85927.1, ECO:0000313|Proteomes:UP000051260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUJ85927.1,
RC ECO:0000313|Proteomes:UP000051260};
RG Swine Surveillance;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; CYUD01000001; CUJ85927.1; -; Genomic_DNA.
DR RefSeq; WP_058280178.1; NZ_CYUD01000001.1.
DR AlphaFoldDB; A0A0P1IB83; -.
DR STRING; 1715692.RUE5091_00405; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000051260; 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:UniProtKB-EC.
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, ECO:0000313|EMBL:CUJ85927.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 578..708
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 708 AA; 77396 MW; DE0DAF2BE9AD9A8A CRC64;
MTDTNEWRAL AEKELRGRPL ADLTKETLEG IEVKPLYTQE DTADLPHIGN LPGFGPFTRG
VKATMYTGRP WTVRQYAGFS TAEESNAFYR SNLAAGQQGI SVAFDLATHR GYDSDHPRVV
GDVGKAGVAI DSVEDMKALF DGIPLDKVTV SMTMNGAVVP ILASFIVAGE EQGHDKSVLA
GTIQNDILKE FMVRNTYVYP PEPSIRIISD IIAYTSNEMP KFNSISISGY HMQEAGGNLV
QELAYTLADG REYVRTAINA GLDVDKFAGR LSFFFGMGMN FFMEIAKLRA ARTLWHRVMT
EFDAKNDRSK MLRTHCQTSG VSLQEQDPYN NVIRTAYEAM SAVLGGTQSL HTNALDEAIA
LPTEFSARIA RNTQLILQEE TGVTDVIDPL AGSYYIESLT NELVEKAWAL MEEVEEMGGM
TKAVASGMPK LRIEESAARR QAMIDRGDEV IVGVNKYRKE KEDPIEILDV DNVVVREAQI
AKLKKMREMR DELACQAALD ELTRRAKEGG NLLEAAVEAA RARASLGEIT MAMEKEFGRH
RAEVKTLAGV YGAAYEGDEG FAAIQEAIEK FAEAEGRRPR LLVVKMGQDG HDRGAKVIAT
AFADIGFDVD VGPLFQTPAE AAQDAVDNDV HVVGISSQAA GHKTLAPLLV EELKKAGAED
IIVICGGVIP QQDYQFLYDH GVKAIFGPGT NIPEAAQDIL RLIGEAKG
//
