ID M0MHR0_9EURY Unreviewed; 292 AA.
AC M0MHR0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cobalt-precorrin-2 C(20)-methyltransferase {ECO:0000313|EMBL:EMA44878.1};
DE EC=2.1.1.151 {ECO:0000313|EMBL:EMA44878.1};
GN ORFNames=C449_09484 {ECO:0000313|EMBL:EMA44878.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA44878.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA44878.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA44878.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA44878.1}.
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DR EMBL; AOMD01000021; EMA44878.1; -; Genomic_DNA.
DR RefSeq; WP_006077749.1; NZ_AOMD01000021.1.
DR AlphaFoldDB; M0MHR0; -.
DR STRING; 1227455.C449_09484; -.
DR PATRIC; fig|1227455.4.peg.1942; -.
DR InParanoid; M0MHR0; -.
DR OrthoDB; 23546at2157; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0043781; F:cobalt-factor II C20-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11645; Precorrin_2_C20_MT; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR012382; CobI/CbiL.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43467:SF2; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00839; SUMT_1; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:EMA44878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011669};
KW Transferase {ECO:0000313|EMBL:EMA44878.1}.
FT DOMAIN 2..195
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 220..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 30692 MW; FBCE37EBA5007642 CRC64;
MTLYGVGLGP GEADLLTIRG KRVLETADVV YSPGRLSRSV AVEHVSDERI GDLDFPMTRD
EEELRRAWRA AALEIAPRAR DGTAAFVTLG DPNVYSTFGH LRRTLAAFHP DVGIEIVPGV
SAVTAFATAL GVEIAAGASL ALREAARGAA PTGPDRMILF KVTDAPTTHE GLHEVGYDVV
YGRRLFMEQG ETIVTEDPDA IAERDYYTLA YAEKHDLDTT PATGAFEKDE SAGVPVAESG
AETSDGGSDG PSRTAADARA GTTDSHGAGS VAVAECAEGE GCGDETPEVR SR
//
