ID A0A1Y5RPW8_9RHOB Unreviewed; 655 AA.
AC A0A1Y5RPW8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:SLN22595.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:SLN22595.1};
GN Name=scpA_2 {ECO:0000313|EMBL:SLN22595.1};
GN ORFNames=PEL8287_00985 {ECO:0000313|EMBL:SLN22595.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN22595.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN22595.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN22595.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFL01000002; SLN22595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RPW8; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000193827; 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 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:SF3; COENZYME B12-DEPENDENT MUTASE; 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:SLN22595.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT DOMAIN 521..650
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 655 AA; 71797 MW; AB341463AB69E255 CRC64;
MSQTQKDRPW LIRTYAGHST ASASNALYRA NLAKGQTGLS VAFDLPTQTG YDSDHVLARG
EVGKVGVPVC HLGDMRALFD QIPLDQMNTS MTINATAPWL LALYIAVAEE QGADVAALQG
TVQNDLIKEY LSRGTYICPP KPSLKMIGDV AEYCYKNVPK WNPMNVCSYH LQEAGATPEQ
ELAFALATAT AVLDELKPRV AAQDFPALAG RISFFVNAGI RFVTEMCKMR AFVDLWDEIL
HTRYGVKDPK FRRFRYGVQV NSLGLTEQQP ENNVYRILIE MLAVTLSKKA RARAVQLPAW
NEALGLPRPW DQQWSMRMQQ ILAYETDLLE FDDLFEGNPA VDAKVEALKD GARHELANLD
SMGGAISAIE YMKSRLVDSN AERLNRIERN ETVVVGVNKW TTTEPSPLQT EDGGIMIVDP
AVEAEQIGRL NDWRSQRDAG AVKQALADLR AAASEGRNVM EPSIAAARAG VTTGEWAAQM
RSVFGEYRGP TGVSANPSNK TEGLDEIRTA VDTVSDRLGR RLKFLVGKPG LDGHSNGAEQ
IAFRARDCGM DIGYEGIRLT PEEIVTAALE DKAHVVGLSI LSGSHMPLVQ DLMTRMRDAG
LAEVPVIVGG IIPDDDAARL LEMGVARVYT PKDFELNTIM MDIVALADPQ AFAAE
//
