ID A0A1Y5SLG4_9RHOB Unreviewed; 711 AA.
AC A0A1Y5SLG4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=scpA_3 {ECO:0000313|EMBL:SLN42342.1};
GN ORFNames=PAM7971_02011 {ECO:0000313|EMBL:SLN42342.1};
OS Pacificibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pacificibacter.
OX NCBI_TaxID=658057 {ECO:0000313|EMBL:SLN42342.1, ECO:0000313|Proteomes:UP000193307};
RN [1] {ECO:0000313|EMBL:SLN42342.1, ECO:0000313|Proteomes:UP000193307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7971 {ECO:0000313|EMBL:SLN42342.1,
RC ECO:0000313|Proteomes:UP000193307};
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; FWFW01000005; SLN42342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SLG4; -.
DR STRING; 658057.SAMN04488032_10466; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000193307; 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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 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:SLN42342.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193307}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 77258 MW; 881937112C6C5F06 CRC64;
MTDRKLWTEL AGKELRGKPV ESLEWDTLEG IKVKPLYDEG DIKDLPHLGN TPGQAPFTRG
VKATMYAGRP WTIRQYAGFS TAEESNAFYR KALDAGQQGV SVAFDLATHR GYDSDHPRVE
GDVGKAGVAI DSVEDMKILF DGIPLDKVSV SMTMNGAVIP ILASFIVTGE EQGHDKALLA
GTIQNDILKE FMVRNTYIYP PEPSMRIIAD IIEYTANEMP KFNSISISGY HMQEAGANLV
QELAFTLADG REYVRTAIKA GMDVDKFAPR LSFFFAIGMN FFMEAAKLRA ARLLWTRVMD
EFDPKLEKSK MLRTHCQTSG VSLQEQDPYN NVIRTAYEAM SAALGGTQSL HTNALDEAIA
LPTEFSARIA RNTQLILQEE TGITNVVDPL AGSYYVESLT AELADKAWEL MEEVETMGGM
TKAVNTGMPK LRIEESAAKR QALIDRGTEV IVGVNKYRKD NEDPIDILDV DNVAVRASQV
ARLKQIRATR DEALMAETLA DLEAAAQSGK GNLLALAVEA ARARATVGEI SMAMEKSFGR
HRAEVKTLAG VYGAAYEGDA GFAQIQKDVE TFAEAEGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPA EAAQDAIDND VHIVGISSQA AGHKTLAPKL IDELKAQGAG
DIIVICGGVI PQQDYAFLKE AGVKAIFGPG TNIPNAAREI LELIGSSPNK S
//
