ID A0A0E3P040_9EURY Unreviewed; 213 AA.
AC A0A0E3P040;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Dimethylsulfide methyltransferase corrinoid protein {ECO:0000313|EMBL:AKB26518.1};
GN ORFNames=MSMTP_3049 {ECO:0000313|EMBL:AKB26518.1};
OS Methanosarcina sp. MTP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB26518.1, ECO:0000313|Proteomes:UP000033049};
RN [1] {ECO:0000313|EMBL:AKB26518.1, ECO:0000313|Proteomes:UP000033049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTP4 {ECO:0000313|EMBL:AKB26518.1,
RC ECO:0000313|Proteomes:UP000033049};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC {ECO:0000256|ARBA:ARBA00010854}.
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DR EMBL; CP009505; AKB26518.1; -; Genomic_DNA.
DR RefSeq; WP_048181820.1; NZ_CP009505.1.
DR AlphaFoldDB; A0A0E3P040; -.
DR STRING; 1434100.MSMTP_3049; -.
DR GeneID; 24858515; -.
DR KEGG; metm:MSMTP_3049; -.
DR PATRIC; fig|1434100.4.peg.4070; -.
DR HOGENOM; CLU_082102_2_0_2; -.
DR OrthoDB; 134276at2157; -.
DR Proteomes; UP000033049; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02070; corrinoid_protein_B12-BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR036594; Meth_synthase_dom.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF02607; B12-binding_2; 1.
DR SMART; SM01018; B12-binding_2; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF47644; Methionine synthase domain; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51337; B12_BINDING_NTER; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:AKB26518.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033049};
KW Transferase {ECO:0000313|EMBL:AKB26518.1}.
FT DOMAIN 1..92
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 92..213
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 213 AA; 23100 MW; DED731EDC075EF5A CRC64;
MAARDEILNS LAEAVVKGDA SKCVELANKA LENNVDAYDA VINGCANGMS IVSDKYEKRE
MFVPEILLAA RAMQGAVEIF KPHIKADEIK ESGRVAIGVV LGDIHDIGKN LVKLLLETAG
LTVFDLGKDV LPEDFQDKIK EEHVDLVALS ALMTTSMMEM KEDVKLFKEE FPGIKIMVGG
APVSQEFCDN IGADGYADNA SEAIRVAQRL LSE
//
