ID C0ZZL2_RHOE4 Unreviewed; 750 AA.
AC C0ZZL2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mutB {ECO:0000313|EMBL:BAH33797.1};
GN OrderedLocusNames=RER_30890 {ECO:0000313|EMBL:BAH33797.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH33797.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH33797.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000290};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; AP008957; BAH33797.1; -; Genomic_DNA.
DR RefSeq; WP_019748436.1; NC_012490.1.
DR AlphaFoldDB; C0ZZL2; -.
DR GeneID; 57486972; -.
DR KEGG; rer:RER_30890; -.
DR PATRIC; fig|234621.6.peg.3592; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_11; -.
DR Proteomes; UP000002204; Chromosome.
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:BAH33797.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 616..748
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 750 AA; 80735 MW; 79181D9CD634E66B CRC64;
MTTREVKHVI GSFAEVPLED PQSPAPTPPS VEQAQALIEE GANANNYAAE QVVWSTPEGI
DVKPVYTGAD RTAAAESGYP LDSFPGAAPF LRGPYPTMYV NQPWTIRQYA GFSTAAESNA
FYRRNLAAGQ KGLSVAFDLA THRGYDSDHP RVAGDVGMAG VAIDSILDMR QLFDGIDLSQ
VSVSMTMNGA VLPILALYVA AAGEQGVTPD KLAGTIQNDI LKEFMVRNTY IYPPKPSMRI
ISDIFAYSSA EMPKYNSISI SGYHIQEAGA TADLELAYTL ADGVEYIRAG LDAGMDIDKF
APRLSFFWAI GMNFFMEVAK LRAGRLLWAE LVAKFDPKSA KSLSLRTHSQ TSGWSLTAQD
VFNNVPRTCV EAMAATQGHT QSLHTNALDE AIALPTDFSA RIARNTQLLL QQESGTVRPI
DPWGGSYYVE WLTNELANRA RKHIEEVEEA GGMAQAINEG IPKLRIEEAA ARTQARIDSG
RQPLVGVNKY VPDEVDTIEV LKVENSKVRK EQLEKLVRLR AERDPEAVEA ALANLTRAAA
STEGGMENNL LALAVVAARA MATVGEISDA LEKVYGRHQA EIRTISGVYR DEAGTVSNIS
KAMELVEKFA EDEGRRPRIL VAKMGQDGHD RGQKVISTAF ADIGFDVDVG PLFQTPEEVA
NQAADNDVHV VGVSSLAAGH LTLVPALREA LAAAGRPDIM IVVGGVIPPG DFDELYEAGA
AAIFPPGTVI ADAASGLLEK LSAQLGHDHS
//
