ID   A0A0D2U3B2_CAPO3        Unreviewed;       698 AA.
AC   A0A0D2U3B2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=CAOG_001101 {ECO:0000313|EMBL:KJE89666.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE89666.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) 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; KE346360; KJE89666.1; -; Genomic_DNA.
DR   RefSeq; XP_004365972.2; XM_004365915.2.
DR   AlphaFoldDB; A0A0D2U3B2; -.
DR   STRING; 595528.A0A0D2U3B2; -.
DR   EnsemblProtists; KJE89666; KJE89666; CAOG_001101.
DR   GeneID; 14902808; -.
DR   InParanoid; A0A0D2U3B2; -.
DR   OrthoDB; 304517at2759; -.
DR   PhylomeDB; A0A0D2U3B2; -.
DR   Proteomes; UP000008743; 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; 2.
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:UP000008743}.
FT   DOMAIN          563..695
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   698 AA;  76759 MW;  E7FE1A7D85AEBDAA CRC64;
     MTAGGRKAML STSAMAMAQR EQLPLHPTWD KLAQKETKGD TNKLMWKTPE GVTLKPMYSK
     RDTADIPEEV PGVFPFTRGP YATMYTQRPW TIRHYDSDNP RVYGDVGMAG VAIDSVEDMK
     VLFQGIPLDK MSVSMTMNGA VLPVLAMYII AAEEQGVEQK LLQGTVQNDI LKEFMVRNTF
     IYPPEPSMRV IGDIFSYTAQ HMPKYNSISI SGYHIQEAGA DSVLEMAFTI ADGIEYVRTG
     LKAGMSVDDF APRLSFFWAI GMNFYMEIAK MRAARRLWAE LIKEKFSPKS EKSLLLRTHC
     QTSGWSLTEQ DPYNNVIRTT IEAMAAVFGG TQSLHTNALD EALGLPTVFS ARIARNTQII
     IQEESGIPKI ADPWGGSYMM ESLTNQVYDA ALTIIREVED LGGMAKAVES GMPKLRVEES
     AAKRQARIDS NREIIVGVNK YRLEQEERVD VLAVDNSRVR ASQIAKLAEL RAKRDPAKAQ
     AALDALTEAA RTGTGNVLDL SIKAARLRCS VGEISYALEK IWGRHRPVDR MVSGAYKSEF
     GDPKEIEDTI KLVETFANKE GRRPRLLVAK MGQDGHDRGA KVIATGFADL GFDVDIGPLF
     QTPEEVARQA IDADVHVVGA SSQAAGHKTL VPALIEALKK ANRSDILVIC GGVIPPQDYD
     FLYQAGVSAI FGPGTKVPVA ARDVVKAIEA KRVESATA
//