ID B7XBM0_EUGGR Unreviewed; 717 AA.
AC B7XBM0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=MCM {ECO:0000313|EMBL:BAH03574.1};
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039 {ECO:0000313|EMBL:BAH03574.1};
RN [1] {ECO:0000313|EMBL:BAH03574.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20379701; DOI=10.1007/s00203-010-0572-x;
RA Miyamoto E., Tanioka Y., Nishizawa-Yokoi A., Yabuta Y., Ohnishi K.,
RA Misono H., Shigeoka S., Nakano Y., Watanabe F.;
RT "Characterization of methylmalonyl-CoA mutase involved in the propionate
RT photoassimilation of Euglena gracilis Z.";
RL Arch. Microbiol. 192:437-446(2010).
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; AB443637; BAH03574.1; -; mRNA.
DR AlphaFoldDB; B7XBM0; -.
DR BRENDA; 5.4.99.2; 2197.
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 2: Evidence at transcript level;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAH03574.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 592..717
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 717 AA; 78251 MW; B27C326FDC9A8429 CRC64;
MLRKFRPLCI DLPPKWVEMA NKELKGKGTV DKLLWNTPEG ITVKPIYTAE DIKEHRSLPG
VFPYTRGPHA SMYTIRPWTI RQYAGFSTVE ESNAFYKKAI AAGQQGLSVA FDLPTHRGYD
SDHPRVEGDV GMAGVAVDSV EDMKLLFDGI PLEKMSVSMT MNGAALPILA MYIVAGEEQG
ADKAKMSGTI QNDILKEFMV RNTYIYPAEI SITIIAHIMG YLAKNMPKYN SISISGYHLQ
EAGAHAALEL GFTIADGLEY INAALKAGLT VDEIAPRLSF FFGIGMNFYM EVAKLRAARQ
LWATKVKELF QPKSAKSLLL RTHCQTSGWS LTEQDPYNNI IRTTVEAMAA VMGGTQSLHT
NSFDEAIALP TPFSSRIARN TQLIIQEETG ITKVVDPWAG SYAMEKLTDD LIVEATKVID
EVQLLGGMTK AINSGMPKLR IEESAARKQA RIDSGADVIV GVNKYTIPQD GESVEVLSID
NTIVRKKQVE RLSKIRATRD SAAVEKALDA ITECARNGEG NLLDLAVIAA RARATVGEIS
LAIEKVHGRY VAGTNVVSGV YLSEYENNIK DKGGIESIRK KVEAFEAKHG RRPRILVCKM
GQDGHDRGAK VVSTGFADMG FDVDVGPLFQ TPAEVARHAV EADVHIVGVS TQAAGHKTRV
PQLINELKSQ NASDILVIVG GVIPQKDYDA LYEAGVSLVF GPGTRLPEAA EKVLNKL
//
