ID W0I716_9EURY Unreviewed; 144 AA.
AC W0I716;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Methylmalony-CoA mutase {ECO:0000313|EMBL:AHF80507.1};
GN ORFNames=TES1_1123 {ECO:0000313|EMBL:AHF80507.1};
OS Thermococcus paralvinellae.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF80507.1, ECO:0000313|Proteomes:UP000019027};
RN [1] {ECO:0000313|EMBL:AHF80507.1, ECO:0000313|Proteomes:UP000019027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES1 {ECO:0000313|EMBL:AHF80507.1,
RC ECO:0000313|Proteomes:UP000019027};
RX PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
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DR EMBL; CP006965; AHF80507.1; -; Genomic_DNA.
DR RefSeq; WP_042681060.1; NZ_CP006965.1.
DR AlphaFoldDB; W0I716; -.
DR STRING; 582419.TES1_1123; -.
DR GeneID; 24907514; -.
DR KEGG; ths:TES1_1123; -.
DR HOGENOM; CLU_128233_0_0_2; -.
DR OrthoDB; 9041at2157; -.
DR Proteomes; UP000019027; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR PANTHER; PTHR48101:SF1; METHYLMALONYL-COA MUTASE, LARGE SUBUNIT; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 6..137
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 144 AA; 15740 MW; 7E313745F34AA3CF CRC64;
MVERSKVRVV IAKPGLDGHD RGAKVVARAL RDAGFEVIYT GIRQTPEQIV ETVIQEDAAV
LGISILSGAH MVLIPKILKL LEERGLKINE DVVVFAGGII PPDDAEELKK MGVAEVFGPG
TPLNKVIEFI DESVKNLKRF KEET
//
