ID A0A212R9P7_9PROT Unreviewed; 726 AA.
AC A0A212R9P7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ORFNames=SAMN07250955_106258 {ECO:0000313|EMBL:SNB68880.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB68880.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB68880.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB68880.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FYEH01000006; SNB68880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212R9P7; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000197065; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000197065}.
FT DOMAIN 589..721
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 726 AA; 78085 MW; B63822A6AAA489F8 CRC64;
MSRIPDFWAL DLDAACDGLD SSTSSMETAP HWSTPEGIGV KAAYGPEDIA DLAAPASLPG
QEPFLRGPYP TMYTTQPWTI RQYAGFSTAE ESNAFYRRNL AMGQKGLSIA FDLATHRGYD
SDHPRVRGDV GMAGVAVDSI LDMRTLFAGI PLERMTVSMT MNGAVLPVLA LFIVAGLEQG
VPEERLAGTI QNDILKEFMV RNTYIFGPVP SMRIITDIFA YTAARMPRFN SISISGYHMQ
EAGATADLEL AYTLADGIEY VRAGIAAGLN VDAFAPRLSF FFAIGMNVAM EIAKLRAARL
LWAELMRAHF QPGSKKSLLL RTHCQTSGWS LTARDVQNNV VRTCLEAMAA TWGGTQSLHT
NAYDEALALP SARSARIARN TQLFLQSEAG FTRTIDPWGG SFYIERLTAD LAAAARRHIA
EIEAAGGMTQ AIVAGIPKLR IEEAAARTQA RIDSGRQTVV GVNRFQPRAE APVEVLRIDN
ESVRQRQLDS LARLRSERDG RAVQAALAEL TQRASGQGNL LEAAIRAARL GATVGEMTAA
LEAVWPRHVA PIQAISGVYG REMAMDNEAE RLAETRALVE RFAEADGRRP RILLAKMGQD
GHDRGQKVIA TAFADLGFDV DIGPLFQTPA EAAGQAVDND VHVVGVSSLA GGHRALVPEL
QAALARAGGR HIMIVVGGVV PPEDYTALRK AGAALIFGPG TAIPEAAAEL LRCLASHLGY
RLDAVG
//
