ID A5P6R3_9SPHN Unreviewed; 718 AA.
AC A5P6R3;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=ED21_26123 {ECO:0000313|EMBL:EDL50014.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL50014.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL50014.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL50014.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDL50014.1}.
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DR EMBL; ABCG01000001; EDL50014.1; -; Genomic_DNA.
DR RefSeq; WP_006831828.1; NZ_ABCG01000001.1.
DR AlphaFoldDB; A5P6R3; -.
DR STRING; 161528.ED21_26123; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000005498; 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:EDL50014.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005498}.
FT DOMAIN 577..709
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 718 AA; 77824 MW; 39769FE4A1DC1359 CRC64;
MTDKPTYDDW KTRADKEVKG RDLTWNTPEG IAVKPLYTSA DTADLDPGVP GIAPFTRGPY
ASMYTGRPWT IRQYAGFSTA EESNAFYRRN LAAGQKGLSV AFDLATHRGY DSDHPRVVGD
VGKAGVAIDT VRDMEILFDQ IPLDTMSVSM TMNGAVIPVL AFYIVAAERQ GVSQDKLAGT
IQNDILKEFM VRNTYIYPPE PSMRIVSDII AYTSANMPKF NSISISGYHM HEAGATAVQE
LAFTIADGKE YAKRAMEAGL DIDAFAPRLS FFWGIGMNFF MEIAKMRAAR ALWHDVMEGL
GAQNPKSKML RTHCQTSGVS LQEQDPYNNV IRTTIEAMAA VLGGTQSLHT NALDEAIALP
TDFSARIARN TQLVIQEETG ITNVADPLGG SYYIESLTAA LVDEASKLLD EVESAGGMTR
YVASGKPKAQ IEQAAAAKQA SVDRGETVIV GVNKYRRDKE DEIDTLDIDN HAVRQSQIAR
LEKVRANRDE FACKAALDAL ARGAAQREGN LLDLAVEAAR HDATLGEISQ AMEDAYGRYD
TNPKPVRGIY SEAYAGDDRY AQVVEGVKAV ERRLGRAPKL MVAKMGQDGH DRGANVIASA
FADMGFEVVS GPLFQTPEET RDMALENDVD AIGASSLAAG HKTLIPELIG LLKNSGRSDI
KVIAGGVIPQ KDYDFLRDAG VQGIYGPGSN VVECAADVLR LLGHNMPPAG EDLDEAAE
//
