ID A0A160F444_9BACI Unreviewed; 141 AA.
AC A0A160F444;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methylmalonyl-CoA epimerase {ECO:0000313|EMBL:ANB61177.1};
DE EC=5.1.99.1 {ECO:0000313|EMBL:ANB61177.1};
GN Name=mce {ECO:0000313|EMBL:ANB61177.1};
GN ORFNames=GFC30_2551 {ECO:0000313|EMBL:ANB61177.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61177.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB61177.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61177.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.
CC {ECO:0000256|ARBA:ARBA00009308}.
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DR EMBL; CP015438; ANB61177.1; -; Genomic_DNA.
DR RefSeq; WP_066326078.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A160F444; -.
DR KEGG; aamy:GFC30_2551; -.
DR PATRIC; fig|294699.3.peg.2625; -.
DR OrthoDB; 9788468at2; -.
DR Proteomes; UP000076865; Chromosome.
DR GO; GO:0004493; F:methylmalonyl-CoA epimerase activity; IEA:UniProtKB-EC.
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 Isomerase {ECO:0000313|EMBL:ANB61177.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865}.
FT DOMAIN 5..133
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 141 AA; 15321 MW; 50367C0727814ED7 CRC64;
MNIKKVDHIG IAVSSIEKAL PFYVDILQLE LLGLEEVESE KVKVAFLKVG DVKLELLEPT
SPDSAVAAFI AKRGEGIHHV ALGVDDIQAR IDELKANGIR MIHEAPKTGA GGALVAFMHP
KSAYGVLYEL CERTDKGVHH E
//
