ID   B3QAM5_RHOPT            Unreviewed;       719 AA.
AC   B3QAM5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   OrderedLocusNames=Rpal_2039 {ECO:0000313|EMBL:ACF00562.1};
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF00562.1, ECO:0000313|Proteomes:UP000001725};
RN   [1] {ECO:0000313|EMBL:ACF00562.1, ECO:0000313|Proteomes:UP000001725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1 {ECO:0000313|EMBL:ACF00562.1,
RC   ECO:0000313|Proteomes:UP000001725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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}.
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DR   EMBL; CP001096; ACF00562.1; -; Genomic_DNA.
DR   RefSeq; WP_012495379.1; NC_011004.1.
DR   AlphaFoldDB; B3QAM5; -.
DR   KEGG; rpt:Rpal_2039; -.
DR   HOGENOM; CLU_009523_3_1_5; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000001725; 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:ACF00562.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          582..714
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   719 AA;  78118 MW;  E041ED58215405C6 CRC64;
     MSKIPNFAEI AFQPTAAPAP AGEAQPWLTP EGILVKPGYS EADVAGIDFL DTWPGVAPFL
     RGPYPTMYVN QPWTIRQYAG FSTAEDSNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDHPR
     VAGDVGMAGV AIDSIYDMRT LFAGIPLDQM SVSMTMNGAV LPILALYVAA AEEQGVSPEK
     LSGTIQNDIL KEFMVRNTYI YPPVPSMRII SDIFAYTSQK MPKFNSISIS GYHMQEAGAT
     QDLELAYTLA DGVEYVRAGI AAGLDVDKFA PRLSFFWAIG MNFFMEVAKM RAARLLWAKL
     LTQFDPKQQK SLSLRTHCQT SGWSLTAQDV FNNVSRTTIE AMAATQGHTQ SLHTNALDEA
     LALPTDFSAR IARNTQLFLQ QESGTTRIID PWGGSYYVER LTHDIAVKAW AHIQEVEALG
     GMAKAIEAGV PKLRIEEAAA KTQARIDTGR QSVIGVNKYK PTDETPIDVL KVDNSTVRRL
     QIDKLGRLKK ERVQADVDAA LLALTRSASE GNGNLLALAI DAARKKATVG EISDALEKVY
     GRHRAEIKSI TGVYKREVAS MADRMEKVQA LIDAFEDAEG RRPRILVAKI GQDGHDRGQK
     VIASAFADIG FDVDIGPLFA TAEEAARQAV ENDVHILGVS SLAAAHLTAV PELKAALKKQ
     GREDIMIIIG GVVPPQDYDA LYKSGAEAIF PPGTVIADAA EELIHKLNAR LGHSSQAAE
//