ID   MCE_PYRHO               Reviewed;         136 AA.
AC   O58010; Q977P4;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Methylmalonyl-CoA epimerase;
DE            EC=5.1.99.1;
DE   AltName: Full=DL-methylmalonyl-CoA racemase;
GN   OrderedLocusNames=PH0272;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=11481338; DOI=10.1074/jbc.m107232200;
RA   Bobik T.A., Rasche M.E.;
RT   "Identification of the human methylmalonyl-CoA racemase gene based on the
RT   analysis of prokaryotic gene arrangements. Implications for decoding the
RT   human genome.";
RL   J. Biol. Chem. 276:37194-37198(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [3]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14586582; DOI=10.1007/s00253-003-1474-5;
RA   Bobik T.A., Rasche M.E.;
RT   "Purification and partial characterization of the Pyrococcus horikoshii
RT   methylmalonyl-CoA epimerase.";
RL   Appl. Microbiol. Biotechnol. 63:682-685(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA;
CC         Xref=Rhea:RHEA:20553, ChEBI:CHEBI:57326, ChEBI:CHEBI:57327;
CC         EC=5.1.99.1; Evidence={ECO:0000269|PubMed:11481338,
CC         ECO:0000269|PubMed:14586582};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=79 uM for (S)-methylmalonyl-CoA {ECO:0000269|PubMed:14586582};
CC         Vmax=467 umol/min/mg enzyme toward (S)-methylmalonyl-CoA
CC         {ECO:0000269|PubMed:14586582};
CC         Note=kcat is 240 sec(-1) for (S)-methylmalonyl-CoA epimerization.;
CC       Temperature dependence:
CC         Highly thermostable: is fully active after 60 minutes at 100 degrees
CC         Celsius and loses less than 10 per cent of its activity after 100
CC         minutes at the same temperature. {ECO:0000269|PubMed:14586582};
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AF364548; AAK52053.1; -; Genomic_DNA.
DR   EMBL; BA000001; BAA29344.1; -; Genomic_DNA.
DR   PIR; A71452; A71452.
DR   AlphaFoldDB; O58010; -.
DR   SMR; O58010; -.
DR   STRING; 70601.3256661; -.
DR   EnsemblBacteria; BAA29344; BAA29344; BAA29344.
DR   KEGG; pho:PH0272; -.
DR   eggNOG; arCOG02706; Archaea.
DR   OMA; IHHICYE; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004493; F:methylmalonyl-CoA epimerase activity; IDA:UniProtKB.
DR   GO; GO:0046491; P:L-methylmalonyl-CoA metabolic process; IDA:UniProtKB.
DR   CDD; cd07249; MMCE; 1.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR017515; MeMalonyl-CoA_epimerase.
DR   InterPro; IPR037523; VOC.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   TIGRFAMs; TIGR03081; metmalonyl_epim; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Isomerase; Metal-binding.
FT   CHAIN           1..136
FT                   /note="Methylmalonyl-CoA epimerase"
FT                   /id="PRO_0000429140"
FT   DOMAIN          7..134
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         10
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        136
FT                   /note="E -> G (in Ref. 1; AAK52053)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   136 AA;  15408 MW;  6615224261DF362F CRC64;
     MIWMFKRIDH VGIAVKNLEE AIKIWEGLGF KVEEIEEVPD QKVKVAVIKV GENRIELLEA
     TTEDSPIAKF IEKRGEGIHH LAIRVENIES KLEELKQKGY KLIDEKPRVG AGGAKIAFIH
     PKSVTGVLLE LCERKE