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Database: UniProt
Entry: A0A0J1F6I4_9FIRM
LinkDB: A0A0J1F6I4_9FIRM
Original site: A0A0J1F6I4_9FIRM 
ID   A0A0J1F6I4_9FIRM        Unreviewed;       229 AA.
AC   A0A0J1F6I4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Cobalt-precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:KLU58985.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:KLU58985.1};
GN   Name=cbiH {ECO:0000313|EMBL:KLU58985.1};
GN   ORFNames=CEB3_c50050 {ECO:0000313|EMBL:KLU58985.1};
OS   Peptococcaceae bacterium CEB3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU58985.1, ECO:0000313|Proteomes:UP000035957};
RN   [1] {ECO:0000313|EMBL:KLU58985.1, ECO:0000313|Proteomes:UP000035957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEB3 {ECO:0000313|EMBL:KLU58985.1,
RC   ECO:0000313|Proteomes:UP000035957};
RA   Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA   Muehling M.;
RT   "Genome sequence of the moderately acidophilic sulfate reducing
RT   Peptococcaceae bacterium strain CEB3.";
RL   Submitted (JUN-2015) 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:KLU58985.1}.
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DR   EMBL; LDXJ01000064; KLU58985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1F6I4; -.
DR   STRING; 999898.CEB3_c50050; -.
DR   PATRIC; fig|999898.3.peg.5594; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000035957; 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:KLU58985.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035957};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KLU58985.1}.
FT   DOMAIN          1..180
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   229 AA;  25037 MW;  9A9A1A584B37E236 CRC64;
     MTGRAKEALA EADTVAGYKT YIDLIRPFLK RQEIVATGMR QEVERCREVV RLASQGRRVA
     LVSSGDAGIY GMAGILIECL SEADRLDLPL EIVPGITAAN AAAAVLGAPL MHDFAAISLS
     DLLTPWEVIV RRVHLAAEGD FVIALYNPKS RGRTEQIEII REVLLKYRAP ETPVGIVREA
     LRGPGCTAVI RTLANFTQEK IDMLTTVIIG NSQTRRLGPY LVTARGYHL
//
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