ID   CBID_LISMC              Reviewed;         373 AA.
AC   C1L299;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=Lm4b_01198;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS04965.1; -; Genomic_DNA.
DR   RefSeq; WP_003724728.1; NC_012488.1.
DR   AlphaFoldDB; C1L299; -.
DR   SMR; C1L299; -.
DR   KEGG; lmc:Lm4b_01198; -.
DR   HOGENOM; CLU_041273_1_0_9; -.
DR   OMA; YHGKLIK; -.
DR   BioCyc; LMON568819:LM4B_RS05980-MON; -.
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..373
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000212939"
SQ   SEQUENCE   373 AA;  40284 MW;  33CE83C9691E7158 CRC64;
     MEDFIYYNGK KYRKGYTTGT CAAAAAKACV EMILTQEEVS AVQVTTTGGT ILEIPVAYQK
     FSKDKATAAV QKDGGDDIDA THGMWIFVDV DLTDNAEVVL DGGVGIGRAT QKGISVAVGE
     AAINPAPRKN ILATVRESLG ENRGAKILVY APEGEERAKR TMNSNLGIIG GISILGTTGI
     VTPMSDEGWK KSLSMELEMK RNQGLDQIIL VPGNYGDDFV QNTLGFSSGN IVSMSNFVGY
     MLKETQRLAF KKVLMVGHFG KLVKVSAGIF TTYSKDADAR AEILVANLAL LGAPLSLLQA
     VEKCNTTEAA GELIEEAGFT QVYDVIVQKI KARSERFLKF TKPSVEVDVV TFSTERGLLA
     ATKDIDVLRE EWR