ID A0A429AXP2_9ACTN Unreviewed; 714 AA.
AC A0A429AXP2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DMB42_29995 {ECO:0000313|EMBL:RSN05012.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN05012.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN05012.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN05012.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSN05012.1}.
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DR EMBL; QHHZ01000011; RSN05012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429AXP2; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000286861; 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.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286861}.
FT DOMAIN 585..714
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 714 AA; 77213 MW; DD022CC6E019EEE6 CRC64;
MIPDFTGVPL DGGSGPGAGA VPEGEVWETP EGIGVKPLYT AADLDGLDFL RTYPGAPPYL
RGPYPTMYVN QPWTIRQYAG FSTAEDSNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDHPR
VAGDVGMAGV AIDSIYDMRQ LFDGIPLDRM SVSMTMNGAV LPVLAMYIVA AEEQGVAPEE
LAGTIQNDIL KEFMVRNTYI YPPTPSMRII SDIFAYTSEK MPKFNSISIS GYHIQEAGAT
CDLELAYTLA DGVEYLRAGI AAGMDVDRFA PRLSFFWCIG MNFFMEVAKL RAARLLWAKL
VARFGAANPR SLSLRTHSQT SGWSLTAQDV FNNVARTCVE AMAATQGHTQ SLHTNALDEA
LALPTDFSAR IARNTQLLLQ QESGTTQVID PWGGSFYVER LTHDLAERAW AHIEEVEAAG
GMARAIEAGL PKLRIEEAAA RTQARIDSGR QPVIGVNKYR AADDEPIEVL KVDNSAVRAQ
QLDKLARLRA ERDGEAVERA LDALTKAAEN PAPGLDANLL KLAVDAARAK ATVGEISDAL
ERVFGRHAEQ VRTISGVYRD ESGPAESIER VRSACADFER HEGRRPRILV AKMGQDGHDR
GQKVIATAFA DLGFDVDVGP LFQTPEEVAR QAVEADVHIV GVSSLAAGHL TLVPALRRAL
ADLDAEDIMI VVGGVIPPGD HDELRAAGAA AIFPPGTVIA DAALDLIQTL RERH
//
