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Database: UniProt
Entry: B3RRT7_TRIAD
LinkDB: B3RRT7_TRIAD
Original site: B3RRT7_TRIAD 
ID   B3RRT7_TRIAD            Unreviewed;       173 AA.
AC   B3RRT7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=VOC domain-containing protein {ECO:0000259|PROSITE:PS51819};
GN   ORFNames=TRIADDRAFT_54362 {ECO:0000313|EMBL:EDV26928.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26928.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV26928.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26928.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.
CC       {ECO:0000256|ARBA:ARBA00009308}.
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DR   EMBL; DS985243; EDV26928.1; -; Genomic_DNA.
DR   RefSeq; XP_002110924.1; XM_002110888.1.
DR   AlphaFoldDB; B3RRT7; -.
DR   STRING; 10228.B3RRT7; -.
DR   EnsemblMetazoa; TriadT54362; TriadP54362; TriadG54362.
DR   GeneID; 6752137; -.
DR   KEGG; tad:TRIADDRAFT_54362; -.
DR   CTD; 6752137; -.
DR   eggNOG; KOG2944; Eukaryota.
DR   HOGENOM; CLU_046006_5_0_1; -.
DR   InParanoid; B3RRT7; -.
DR   OMA; IHHICYE; -.
DR   OrthoDB; 306061at2759; -.
DR   PhylomeDB; B3RRT7; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0004493; F:methylmalonyl-CoA epimerase activity; IBA:GO_Central.
DR   GO; GO:0046491; P:L-methylmalonyl-CoA metabolic process; IBA:GO_Central.
DR   CDD; cd07249; MMCE; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR017515; MeMalonyl-CoA_epimerase.
DR   InterPro; IPR037523; VOC.
DR   NCBIfam; TIGR03081; metmalonyl_epim; 1.
DR   PANTHER; PTHR43048; METHYLMALONYL-COA EPIMERASE; 1.
DR   PANTHER; PTHR43048:SF3; METHYLMALONYL-COA EPIMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF13669; Glyoxalase_4; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          44..173
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   173 AA;  19312 MW;  2062C26C5AF13993 CRC64;
     MASVMRFISL AGRRSWLYYN KVEQLTDESI LRTNKEQAFW KLGKLNHLAI AVPDLEKATA
     FYRDVLGASV SEQLPLPEHG VTTVFIDLGN TKIELLHPLG EQSPIEGFLA KKPEGGMHHI
     CIEVDDIKAA MKDLVSNKIR TLSKEPRIGA HNKPVMFLHP KDCGGVLVEL EEA
//
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