ID   CBID_TOLAT              Reviewed;         378 AA.
AC   C4LFC1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=Tola_1678;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001616; ACQ93288.1; -; Genomic_DNA.
DR   RefSeq; WP_015878759.1; NC_012691.1.
DR   AlphaFoldDB; C4LFC1; -.
DR   SMR; C4LFC1; -.
DR   STRING; 595494.Tola_1678; -.
DR   EnsemblBacteria; ACQ93288; ACQ93288; Tola_1678.
DR   KEGG; tau:Tola_1678; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_1_0_6; -.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000009073; Chromosome.
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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..378
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000212946"
SQ   SEQUENCE   378 AA;  41095 MW;  55DD4ED0517C5309 CRC64;
     MNIALADDKV WHKGKSYRKG YTTGSCATAA AKVATLMILR QQVIHQVSIV TPSGVTLQLN
     VEEPLIHGLQ ASAAIRKDGG DDVDATHGML IYAQVVLRND ATITISGGTG VGKVTRKGIG
     LPVGNAAINK TPLQTIEAAV REVLGPERGA DITIFAPEGE ERAQRTYNGR LGIEGGISII
     GTTGIVTPMS EESWKRSLAL ELEQKRAQGM EKIILVPGNH GERFVREQMQ LDSELVVTMS
     NFVGYMLQEA ERLAFRHVVL IGHLGKLIKV AAGIFHTHSH IADGRMETLI THLALLGAPN
     SLLQAIYACN TTEAAMELIE AQGYQEVYNT IATRICERIN QMLRYSPQPF QCDAILFSLD
     NQPLGSNRPI TDIVEALR