ID A0A0N1LF92_9SPHN Unreviewed; 712 AA.
AC A0A0N1LF92;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=IP68_10740 {ECO:0000313|EMBL:KPF75082.1};
OS Blastomonas sp. AAP25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Blastomonas.
OX NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF75082.1, ECO:0000313|Proteomes:UP000037930};
RN [1] {ECO:0000313|EMBL:KPF75082.1, ECO:0000313|Proteomes:UP000037930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP25 {ECO:0000313|EMBL:KPF75082.1,
RC ECO:0000313|Proteomes:UP000037930};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF75082.1}.
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DR EMBL; LJHP01000011; KPF75082.1; -; Genomic_DNA.
DR RefSeq; WP_054134972.1; NZ_LJHP01000011.1.
DR AlphaFoldDB; A0A0N1LF92; -.
DR PATRIC; fig|1523416.3.peg.516; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000037930; 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:KPF75082.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037930}.
FT DOMAIN 575..707
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 712 AA; 77002 MW; 4CC4C65B69E9BA5C CRC64;
MTDTPNIADW QALAEKEVKG RDLTWHTPEG IAVKPLYTAD DVSVDPGLPG FAPFTRGVRA
SMYAGRPWTI RQYAGFSTAE ESNAFYRRNL AAGQKGLSVA FDLATHRGYD SDHPRVTGDV
GKAGVAIDSV EDMKILFDGI PLDKMSVSMT MNGAVIPILA FFIVAGEEQG VDRKLLDGTI
QNDILKEFMV RNTYIYPPEP SMRIISDIFG YTSREMPKFN SISISGYHMQ EAGATQVQEL
AFTIADGMEY VKYGVASGLD IDKFAGRLSF FFAIGMNFFM EIAKLRAARV LWHRVMTRLG
AQDERSKMLR THCQTSGVSL TEQDPYNNVI RTTIEAMAAM LGGTQSLHTN ALDEAIALPT
DFSARIARNT QIVIQEETGM TNVVDPLGGS YYIESLTQEL VDKAWEIIER VESEGGMAKA
VAAGWPKAMI EEAAAGRQAR VDRAEDVVVG VNKYRLPSED QLDTLDVDNA KVREGQVARI
VSVKASRDAA ACQAALDALR EGAKGDGNLL ALAVDAARAR ATLGEISQAM EDVFGRYATV
PTPVKGVYSA PYVDDGRWAQ VVEGVKAVER RLGRKPKLLV AKMGQDGHDR GANVIASAFG
DLGFEIVSGP LFQTPEETVV LALESNVDVV GASSLAAGHK TLIPSLIAGL KEAGRNDIKV
IVGGVIPPQD YDFLRDAGVQ GIYGPGSNVV ECAADVLRLL GHNMPPLQEA AE
//
