ID   CBIT_METM7              Reviewed;         181 AA.
AC   A6VGG1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00786};
DE            EC=2.1.1.196 {ECO:0000255|HAMAP-Rule:MF_00786};
GN   Name=cbiT {ECO:0000255|HAMAP-Rule:MF_00786}; OrderedLocusNames=MmarC7_0468;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B
CC       followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
CC       {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC         CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00786};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC       CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}.
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DR   EMBL; CP000745; ABR65537.1; -; Genomic_DNA.
DR   RefSeq; WP_011976869.1; NC_009637.1.
DR   AlphaFoldDB; A6VGG1; -.
DR   SMR; A6VGG1; -.
DR   STRING; 426368.MmarC7_0468; -.
DR   EnsemblBacteria; ABR65537; ABR65537; MmarC7_0468.
DR   GeneID; 5329127; -.
DR   KEGG; mmz:MmarC7_0468; -.
DR   eggNOG; arCOG00977; Archaea.
DR   HOGENOM; CLU_094143_0_0_2; -.
DR   OMA; RCKFVYA; -.
DR   OrthoDB; 82864at2157; -.
DR   UniPathway; UPA00148; UER00229.
DR   GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00786; CbiT; 1.
DR   InterPro; IPR023475; CbiT.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..181
FT                   /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT                   /id="PRO_1000046843"
FT   BINDING         16
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         40..44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         61
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
SQ   SEQUENCE   181 AA;  20269 MW;  5D528D5A68019DAE CRC64;
     MIQDSEFFRM EGVPITKEEI RAVSIGKLNL NPEDIVLDIG CGSGGMSVEI SKRSKFVYAI
     DNSEDAKNTT VTNLKKFKIE NCEVFLGDAK DLISEFDFNK VFIGGTQNIE QILEILKEKK
     IEKVVANTIV LENSVKIISK FEELRYNVDF VNVSVSYGKK INSGHIMLSK NPITIITATL
     K