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Database: UniProt
Entry: A0A011QVC9_9PROT
LinkDB: A0A011QVC9_9PROT
Original site: A0A011QVC9_9PROT 
ID   A0A011QVC9_9PROT        Unreviewed;       832 AA.
AC   A0A011QVC9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:EXI93110.1};
DE            EC=5.4.99.2 {ECO:0000313|EMBL:EXI93110.1};
GN   Name=scpA_1 {ECO:0000313|EMBL:EXI93110.1};
GN   ORFNames=AW12_00072 {ECO:0000313|EMBL:EXI93110.1};
OS   Candidatus Accumulibacter sp. BA-94.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI93110.1, ECO:0000313|Proteomes:UP000020878};
RN   [1] {ECO:0000313|EMBL:EXI93110.1, ECO:0000313|Proteomes:UP000020878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI93110.1}.
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DR   EMBL; JEMZ01000003; EXI93110.1; -; Genomic_DNA.
DR   STRING; 1454005.AW12_00072; -.
DR   Proteomes; UP000020878; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR027417; P-loop_NTPase.
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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EXI93110.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020878}.
FT   DOMAIN          533..662
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          792..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  90570 MW;  C9D3D5AFCC0E9FAD CRC64;
     MVAPRKNRDQ PWLMRTYSGH SSAKASNALY RTNLAKGQTG LSVAFDLPTQ TGYDADSPLA
     RGEVGKVGVP ISSIEDMDQL FDQIPLDQMN TSMTINATAA WLLSLYIGLA QRRGIDPKKL
     SGTTQNDIIK EYLSRGTYIY PPGPSMRLIA DTINYTIRHV PKWNPTNVCS YHLQEAGATP
     VQELAYALCT AMAVLDRVKA SGEIGPDEFP LVVERISFFV NAGIRFIEEC CKLRAFGEMW
     DELTLSRYQV EDPKLRRFRY GVQVNSLGLT EAQPENNVQR IVLEMLAVAL SKRARARAIQ
     LPAWNEAMGL PRPWDQQWAL RIQQVMAFET DLLEYGDIFD GSPVIAAKVA ELVEGARREI
     DNVEAQGGII AAIESGYIKR ELVGSHMSRL RAIESGELKI IGLNCFHETA ESPLTAGSDG
     AIMKSDPAAE RQQIERLQEH RRQRSDADVR AALQGLADAA RSGDNIMPSS IRCALAGVTT
     GEWGDSLRAV FGEFRPPTGV DIAIDSREVL GRKDQVTELR ERVGRTGNAL GRPLKILVGK
     PGLDGHSNGA EQVAVKARDV GFEVVYDGIR LTPQQIAQAA QEEGVHVVGL SILSGSHMEL
     VGSVLQELRA RDLAALPVVA GGIIPPADAE RLLALGVRAI YTPKDFNLNA IMGDIVDVVR
     ENNGLERLGS LSCGSARCLE RYMTNLGLPD PEQLAARILR GERSAVASGL NLLDNRLPAA
     RGRAVRLLAC LSGERWLSAG HLIGVTGPPG AGKSSLVSAM IREWRLAXXX XXXXARRSAC
     WRSTRRAGPS WAVARSSATA SASRPRRRTR VSSSARSPIA TSWVGLPARS GR
//
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