ID D8M518_BLAHO Unreviewed; 740 AA.
AC D8M518;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=GSBLH_T00003076001 {ECO:0000313|EMBL:CBK23157.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK23157.2};
RN [1] {ECO:0000313|EMBL:CBK23157.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK23157.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) 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; FN668655; CBK23157.2; -; Genomic_DNA.
DR RefSeq; XP_012897205.1; XM_013041751.1.
DR AlphaFoldDB; D8M518; -.
DR EnsemblProtists; CBK23157; CBK23157; GSBLH_T00003076001.
DR GeneID; 24920199; -.
DR InParanoid; D8M518; -.
DR OMA; IQEETHI; -.
DR OrthoDB; 304517at2759; -.
DR Proteomes; UP000008312; 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.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008312}.
FT DOMAIN 608..740
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 740 AA; 81530 MW; 7E91352E8918745D CRC64;
MLAATRQLAK TSVRAMGICN YPEAWTKIAT KELKGESPET LCFKTPEGIQ MKPMFMKSDL
EGITLDDCSA VFPFTRGPYA TMYTKKPWTI RQYAGFSTAE ASNAFYRKNL AAGQQGLSVA
FDLATHRGYD SDHPRVVGDV GMAGVAIDSV EDMKVLFNGI PLDKMSVSMT MNGAVLPVMA
FYVIAAEEQG VKQELLRGTI QNDILKEFMV RNTFIYPPHE SLRIIQDIMG YTSVHMPKFN
SISISGYHMQ EAGADAMLEM AFTIADGIEY VRTAEAAGVS VDKVAPRLSF FFGIGMNFYM
EVAKLRAARQ LWAKRIQKHF HPQNQKSLLL RTHCQTSGYS LTEQDPYNNI IRTTIEAMAA
VMGGTQSLHT NALDEALGLP TEFSARIARN TQLIIQEETG ICKTVDPWGG SYVIEYLTNQ
LVKGADAIID EVESLGGMTK AIASGMPKLR IEEAAARKQA RIDSGKETIV GVNKYKLAKE
DAVEVREVDN TEVRNSQIAR LKELKAKRDN DAVRRALEAL EYSSKLTEPT GKGTDPNNLM
NLSINAARVR ATLGEISDAL EHHWGRYTPQ QEMVHGAYMQ EYTEDSKTKV FQDVSERAKR
FEEKTGRRPR VYIAKMGQDG HDRGAKVVAT GYADIGFDVD VGPLFQTPAE AARAAVDADV
HVVGCSSLAA GHKTLIPELI ECLKKEGRDD IVVVAGGVIP PKDYDFLYKA GVSAIHGPGT
PITTSANDVL DILEKKNFKL
//
