ID I2JMG6_9GAMM Unreviewed; 719 AA.
AC I2JMG6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DOK_04713 {ECO:0000313|EMBL:EIF44168.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44168.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44168.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44168.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
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:EIF44168.1}.
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DR EMBL; AJMK01000022; EIF44168.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JMG6; -.
DR PATRIC; fig|1168065.3.peg.988; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_6; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000003473; 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:EIF44168.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003473}.
FT DOMAIN 588..719
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 719 AA; 78377 MW; D738AC6117317CA4 CRC64;
MADYKAPETS VDEWKALANK ALAKSNQTLD DLVWHTPEGI DVKPLYTQED VKDLPYTNTL
PGIEPFIRGP QPTMYAGRPW TIRQYAGFST AEESNAFYRK ALAAGGQGVS VAFDLATHRG
YDSDHPRVTG DVGKAGVAID SVEDMKVLFN EIPLDKVSVS MTMNGAVLPV LAGYIVAAEE
QGVPQDKLSG TIQNDILKEF MVRNTYIYPP APSMKIIGDI IAYASSNMPK FNTISISGYH
IQEAGADAAL ELAYTLADGK EYIRTAIAAG LDIDKFAGRL SFFWGIGMNF YMEIAKMRAA
RLLWAKIVSE FEPKDQRSKM LRTHSQTSGW SLTEQDPYNN IVRTTIEAMA AVFGGTQSLH
TNALDEAIAL PTQFSSRIAR NTQLIIQEET GITNVVDPWG GSYMMESLTK DIADRAWELI
QEVEEKGGMA KAIETGLPKL RIEESAARKQ ARIDRGEDVI VGVNKYTLAE EDDVDVLDID
NNAVRESQVA ALAKIRASRD EATVEDALEA IYQCACGGEG NLLDLAVKAT RLRATVGEIS
FAMEREFGRF NAQSQTVSGV YGSAYQDDEN WQGISKDIED FAEKHGRRPR MLVCKMGQDG
HDRGAKVIAT AFADVGFDID LSPMFSTPEE VAKQAVENDV HVVGVSSQAA GHKTLIPELI
SELKKAGADD IIVIAGGVIP RQDYDFLNAA GVKGIFGPGT KIPLAARGVL DAINEAYKG
//
