ID   A0A1Q3RIJ6_9FIRM        Unreviewed;       249 AA.
AC   A0A1Q3RIJ6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Precorrin-4 C(11)-methyltransferase {ECO:0000313|EMBL:OJV63993.1};
GN   ORFNames=BGO41_06995 {ECO:0000313|EMBL:OJV63993.1};
OS   Clostridiales bacterium 38-18.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1895746 {ECO:0000313|EMBL:OJV63993.1, ECO:0000313|Proteomes:UP000185881};
RN   [1] {ECO:0000313|EMBL:OJV63993.1, ECO:0000313|Proteomes:UP000185881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=38-18 {ECO:0000313|EMBL:OJV63993.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}.
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:OJV63993.1}.
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DR   EMBL; MKTL01000007; OJV63993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3RIJ6; -.
DR   STRING; 1895746.BGO41_06995; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000185881; Unassembled WGS sequence.
DR   GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11641; Precorrin-4_C11-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; IPR006362; Cbl_synth_CobM/CibF.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01465; cobM_cbiF; 1.
DR   PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003960};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          3..208
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   249 AA;  27034 MW;  18E79B7F9B63F915 CRC64;
     MKVKFVGAGP GDPELLTIKG HRALSEADTV IYAGSLVNPE LLKYCKSGCE IYNSAVMNLE
     EIIEVCHRDT KAGLSVVRLH TGDFSIYGSL REQIEALNAL DISYELIPGV SSFLGAASAL
     EIEYTVPEIS QSLIITRMEG RTPVPELEKL SSFASHQTSM AIFLSSGMVS DVMTELVKGG
     YTEDTPVAVI YKATWPDEKI VRGSIADIAE KVAEAGISKT ALIIVGRCLG YEFNASKLYD
     KAFSHEFRA
//