ID A0A166RPS9_9RHOB Unreviewed; 709 AA.
AC A0A166RPS9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=A3721_06155 {ECO:0000313|EMBL:KZX98759.1};
OS Sulfitobacter sp. HI0023.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZX98759.1, ECO:0000313|Proteomes:UP000077323};
RN [1] {ECO:0000313|EMBL:KZX98759.1, ECO:0000313|Proteomes:UP000077323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0023 {ECO:0000313|EMBL:KZX98759.1,
RC ECO:0000313|Proteomes:UP000077323};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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:KZX98759.1}.
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DR EMBL; LWEQ01000345; KZX98759.1; -; Genomic_DNA.
DR RefSeq; WP_067927336.1; NZ_LWEQ01000345.1.
DR AlphaFoldDB; A0A166RPS9; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000077323; 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.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077323}.
FT DOMAIN 579..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 709 AA; 77279 MW; FBF3E674F4EF494B CRC64;
MTSDKDTWRN LAEGELRGKP VEDLTWHTLE GIDVQPLYTA EDLEGVDHLG GIPGQAPFTR
GVKATMYAGR PWTIRQYAGF STAEESNAFY RRGLAAGQQG VSVAFDLATH RGYDSDHPRV
EGDVGKAGVA IDSVEDMKIL FDGIPLDKVS VSMTMNGAVI PILASFIVAG EEQGHDRSVL
SGTIQNDILK EFMVRNTYIY PPEPSMRIIG DIIEYTSDHM PKFNSISISG YHMQEAGANL
VQELAFTLAD GREYVRTAIA AGMDVDRFAP RLSFFFAIGM NFFMEAAKLR AARLLWSRIM
SEFEPKNPKS SMLRTHCQTS GVSLSEQDPY NNVVRTAYEA MSAVLGGTQS LHTNALDEAI
ALPTDFSARI ARNTQLILQE ETGVTNVVDP LAGSYYVEKL THDLAEAAWK LIEEVEEMGG
MTQAVASGMP KLRIEEAAAT RQANIDRGTE VVVGVNKYRR DKEDPIDILD VDNVAVRESQ
IARLKRIREE RDDAACRAAL DELTRRAREG GNLLEAAVEA ARARATVGEI SMAMEDEFGR
HRAEVKTLAG VYGAAYEGDE GFAAIQQSVE EFAEAEGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPA EAAQDAVDND VHVIGISSQA AGHKTLAPQL VKALKDAGAE
DILVICGGVI PQQDYEFLYN AGVKAIFGPG TNIPSAAQDI LRLIREARG
//
