ID A0A2M9K304_9ACTN Unreviewed; 682 AA.
AC A0A2M9K304;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=CG723_02740 {ECO:0000313|EMBL:PJN13499.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN13499.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN13499.1}.
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DR EMBL; NNBL01000001; PJN13499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9K304; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000232157; 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 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:SF3; COENZYME B12-DEPENDENT MUTASE; 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:UP000232157}.
FT DOMAIN 543..672
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 682 AA; 74903 MW; 166F47F620F407DD CRC64;
MTERQKDRPW LMRTYAGHST AEASNELYRR NLAKGQTGLS VAFDLPTQTG YDPDHILARG
EVGRVGVPVS HLGDMRRLFQ DIPLEQMNTS MTINATAMWL LALYQVVAEE QGADITQLQG
TTQNDIVKEY LSRGTHVFPP APSLRLTTDM IAYTVRHMPK WNPINICSYH LQEAGATPVQ
EIAYAMSTAI AVLDAVRDSG QVPAEKFGDV VARISFFVNA GVRFIEEMCK MRAFGRIWDQ
ITRERYGIEN AKQRRFRYGV QVNSLGLTEA QPENNVQRIV LEMLAVTLSK DARARAVQLP
AWNEALGLPR PWDQQWSLRI QQVLAHESDL LEYEDIFAGS HVIEKKVDEL VADSFAEIER
IQEMGGAMAA VESGYLKSQL VSSHAERRAR IEGGEEKIVG VNIHESTEPN PLTADLDAAI
MTVDHQVESR VVRAIDEWRT TRQESSDRQG MGDPYHYPTT QQAVERLKAA AAGTENLMEA
TLECARAGVT TGEWSQALRE VFGEFRAPTG VSSAPVAVTA EAGTPLALVR EKVRRTGDEL
GGKLRLLVGK PGLDGHSNGA EQIAVRARDA GFEVVYQGIR LTPEQIVSAA LAEDVHCVGL
SILSGSHAAL VPDVLDRLRE AGAAEIPVIV GGIIPNGDAE DLKRAGVAAV FTPKDFGITE
IIGRIVDEIR QANQLDPLEV PA
//
