ID   CBID_METM6              Reviewed;         365 AA.
AC   A9AAB0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE            EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE   AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN   Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=MmarC6_1470;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC       form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC         EC=2.1.1.195; Evidence={ECO:0000255|HAMAP-Rule:MF_00787};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC   -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00787}.
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DR   EMBL; CP000867; ABX02283.1; -; Genomic_DNA.
DR   RefSeq; WP_012194203.1; NC_009975.1.
DR   AlphaFoldDB; A9AAB0; -.
DR   SMR; A9AAB0; -.
DR   STRING; 444158.MmarC6_1470; -.
DR   PRIDE; A9AAB0; -.
DR   EnsemblBacteria; ABX02283; ABX02283; MmarC6_1470.
DR   GeneID; 5737515; -.
DR   KEGG; mmx:MmarC6_1470; -.
DR   eggNOG; arCOG04383; Archaea.
DR   HOGENOM; CLU_041273_1_0_2; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 57676at2157; -.
DR   PhylomeDB; A9AAB0; -.
DR   UniPathway; UPA00148; UER00227.
DR   GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2110.10; -; 1.
DR   HAMAP; MF_00787; CbiD; 1.
DR   InterPro; IPR002748; CbiD.
DR   InterPro; IPR036074; CbiD_sf.
DR   PANTHER; PTHR35863; PTHR35863; 1.
DR   Pfam; PF01888; CbiD; 1.
DR   PIRSF; PIRSF026782; CbiD; 1.
DR   SUPFAM; SSF111342; SSF111342; 1.
DR   TIGRFAMs; TIGR00312; cbiD; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..365
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000133739"
SQ   SEQUENCE   365 AA;  40017 MW;  39FB0C7AA9BAF99E CRC64;
     MSKIDFRLEK TFGYTTGACA AAGAYSALYF LKNNEKLNFV EILNLKGDSL IIPIKNIEKR
     GNTAVSTVEK FAGEDIDITN GMDIKIEVIL ENWDDGYPKP SNVIIIGGTG VGLITKSGLQ
     IKPGDHAINP KPREMIETNL KSLLKDDEYV TVKISVPTGD EIAKKTLNPK LGIVGGISIL
     GTTGIVRPMS NEAYKESLAP QIDVALANNF ENLIFVPGNI GTKHAKILLN AEEDQIIEVS
     NFWDYMLDKA KEKGVKDIMV FGHAGKIVKL AGGIFDTHSR VADARNEILC AYASLVSQDV
     EMLQKILQSN TTEDIVEILT EKGILSEVFN KVSKRVVERL SLRWEGINFS CIVIDMKGNI
     LGKSD