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Database: UniProt
Entry: U2JSB9_9FIRM
LinkDB: U2JSB9_9FIRM
Original site: U2JSB9_9FIRM 
ID   U2JSB9_9FIRM            Unreviewed;       250 AA.
AC   U2JSB9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:ERJ89156.1};
GN   ORFNames=RUMCAL_03020 {ECO:0000313|EMBL:ERJ89156.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ89156.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ89156.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ89156.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:ERJ89156.1}.
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DR   EMBL; AWVF01000390; ERJ89156.1; -; Genomic_DNA.
DR   RefSeq; WP_021681211.1; NZ_KI260336.1.
DR   AlphaFoldDB; U2JSB9; -.
DR   STRING; 411473.RUMCAL_03020; -.
DR   GeneID; 78474707; -.
DR   PATRIC; fig|411473.3.peg.2539; -.
DR   eggNOG; COG1010; Bacteria.
DR   HOGENOM; CLU_047948_2_0_9; -.
DR   OrthoDB; 9772960at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000016662; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11646; Precorrin_3B_C17_MT; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR   NCBIfam; TIGR01466; cobJ_cbiH; 1.
DR   PANTHER; PTHR47036; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR47036:SF1; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   4: Predicted;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ERJ89156.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERJ89156.1}.
FT   DOMAIN          4..211
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   250 AA;  27247 MW;  19A3DC3A04586907 CRC64;
     MKPKIYVVGF GPGERPYMTQ QAVDAMTQAD LVVGYTTYVR LLEKQFPELQ YYATPMRKEA
     DRCRAAVEAA LTGKTVALVS SGDSGIYGMA GVLLEIAAEM QADVEVIAVA GVTAASAAAA
     VLGAPLMHDF AVISLSDCMT PLEQIYRRVA LAAEADFVIC LYNPKSRSRT AYLAEAAKLI
     QQHRKPETPV GIVRNAGREG KRAWITTLEK LPEEPVDMFC VVLVGNSQTY VQNGKMITPR
     GYCVRREESC
//
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