ID   CBID_METM7              Reviewed;         366 AA.
AC   A6VGE3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=MmarC7_0450;
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-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; CP000745; ABR65519.1; -; Genomic_DNA.
DR   RefSeq; WP_011976851.1; NC_009637.1.
DR   AlphaFoldDB; A6VGE3; -.
DR   SMR; A6VGE3; -.
DR   STRING; 426368.MmarC7_0450; -.
DR   PRIDE; A6VGE3; -.
DR   EnsemblBacteria; ABR65519; ABR65519; MmarC7_0450.
DR   GeneID; 5328998; -.
DR   KEGG; mmz:MmarC7_0450; -.
DR   eggNOG; arCOG04383; Archaea.
DR   HOGENOM; CLU_041273_1_0_2; -.
DR   OMA; YHGKLIK; -.
DR   OrthoDB; 57676at2157; -.
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..366
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000046865"
SQ   SEQUENCE   366 AA;  39981 MW;  17C28B5653A29475 CRC64;
     MGKIDFRLEK TFGYTTGACA AAGAYSALYF LKNNERLNFV EIVNLKEDSL IIPIKNIEKQ
     GDTAISTVEK FSGEDIDITN GMDIEIEVTL NLDNNSSESS NVDIIGGIGV GIITKSGLQV
     TLGKPAINPK PREMIETNLK SLLTDNECVT VKISVPNGDE IAKKTLNPKL GIIGGISILG
     TTGIVRPMSN DAYKESLAPQ IDVALANNFE NLIFVPGNIG TKHAKILLHA EEDQIIEVSN
     FWDYMLNKAK EKGVKDITVF GHAGKIVKLA GGIFDTHSKV ADARNEILCA YTSLVTQDVE
     ILQKILQSNT TEDIVEILTE KGILKEVFDN VSKRVVERLS SRWDGINFSC IIINMKGNML
     GKYDQG