ID A0A238K525_9RHOB Unreviewed; 656 AA.
AC A0A238K525;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:SMX37202.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:SMX37202.1};
GN Name=scpA_1 {ECO:0000313|EMBL:SMX37202.1};
GN ORFNames=PEV8663_00970 {ECO:0000313|EMBL:SMX37202.1};
OS Pelagimonas varians.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=696760 {ECO:0000313|EMBL:SMX37202.1, ECO:0000313|Proteomes:UP000220836};
RN [1] {ECO:0000313|EMBL:SMX37202.1, ECO:0000313|Proteomes:UP000220836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8663 {ECO:0000313|EMBL:SMX37202.1,
RC ECO:0000313|Proteomes:UP000220836};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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; FXYH01000003; SMX37202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238K525; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000220836; 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:SMX37202.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000220836}.
FT DOMAIN 523..651
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 656 AA; 72340 MW; DA82734A650ED892 CRC64;
MTETETQRDR PWLIRTYAGH STAEASNALY RNNLAKGQTG LSVAFDLPTQ TGYDSDHILA
RGEVGKVGVP VCHLGDMRTL FADIPLEQMN TSMTINATAP WLLSLYIAAA EEQGADVSKL
QGTVQNDLIK EYLSRGTYIC PPKPSLKMIG DVAEYCYKHV PKWNPMNVCS YHLQEAGATP
EQELSFALAT AIAVLDELKP RVAEEDFPAL CGRISFFVNA GIRFVTEMCK MRAFVDLWDE
ILLTRYGVEN PKFRRFRYGV QVNSLGLTEQ QPENNVYRIL IEMLAVTLSK NARARAVQLP
AWNEALGLPR PWDQQWSMRM QQILAYETDL LEYEDLFEGN PAVDRKVEAL KDGARAELAN
IDSMSGAIGS IDYMKGRLVE SNADRLSRIE RNETIVVGVN KWTEGEPSPL VGEDGGIMVV
DPAVEQEQIS RLAEWRSARD NDAVQSALAT LRAASVAGEN IMPASIACAK VGVTTGEWAS
QMRAVHGEYR GPTGVSQSVS NKTEGLEDIR SAVDLVSDKL GKRLRFLVGK PGLDGHSNGA
EQIAFRARDC GMEIDYEGIR LTPEQIVEAA REGVHVVGLS ILSGSHIPLV EDVMKRMQDA
DLGHIPVTVG GIIPDEDAER LRAMGVARVY TPKDFELNTI MRDIVSLVDP EKTAAE
//
