ID A0A0A0EGV0_9RHOB Unreviewed; 709 AA.
AC A0A0A0EGV0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=ATO9_05880 {ECO:0000313|EMBL:KGM49550.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM49550.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM49550.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM49550.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
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:KGM49550.1}.
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DR EMBL; AQQX01000002; KGM49550.1; -; Genomic_DNA.
DR RefSeq; WP_043746595.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EGV0; -.
DR STRING; 1461694.ATO9_05880; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000030004; 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:KGM49550.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT DOMAIN 579..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 709 AA; 77565 MW; 94DF5BBE6EEA3B52 CRC64;
MASKKDAWAE LAAKELRGKP LSDLDWETLE GIKVKPLYTE EDTEGLEHMG SMPGFGPFTR
GPKATMYAGR PWTIRQYAGF STAEESNAFY RRNLAAGQQG VSVAFDLATH RGYDSDHPRV
VGDVGKAGVA IDSVEDMKIL FDGIPLDQVS VSMTMNGAVI PILANFIVTG EEQGHDKSVL
SGTIQNDILK EFMVRNTYIY PPQPSMRIIS DIIEYTSNEM PRFNSISISG YHMQEAGANL
VQELAFTLAD GREYVKAAIE AGMDVDKFAG RLSFFFAIGM NFFMEAAKLR AARTLWHRIM
TEFGAEQEKS KMLRTHCQTS GVSLQEQDPY NNVIRTAYEA LSAVLGGTQS LHTNALDEAI
ALPTDFSARI ARNTQLILQE ETGITNVVDP LAGSYYVESL TNELIEKAWA LIEEVEEMGG
MTKAVASGMP KLRIEESAAR RQALIDRGED VIVGVNKYRK DKEDPIDILD VDNVKVRDSQ
VKALERIRAE RDEDACTKAL DELTRRAKEG GNLLEAAVEA ARARATVGEI SMAMEKEFGR
HRAEVKTLAG VYGAAYEGDE GFAAIQKDIE AFAEEEGRRP RLLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPD EAAQDAIDND VHVVGISSQA AGHKTLAPQL IEALKEKDAG
DIIVICGGVI PQQDYDFLKK AGVKAIFGPG TNIPAAAQDI LKLIREARA
//
