ID   CBID_METKA              Reviewed;         409 AA.
AC   Q8TYG5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=MK0334;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01549.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TYG5; -.
DR   SMR; Q8TYG5; -.
DR   STRING; 190192.MK0334; -.
DR   EnsemblBacteria; AAM01549; AAM01549; MK0334.
DR   KEGG; mka:MK0334; -.
DR   PATRIC; fig|190192.8.peg.355; -.
DR   HOGENOM; CLU_041273_1_0_2; -.
DR   OMA; YHGKLIK; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001826; 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.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..409
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_0000141693"
SQ   SEQUENCE   409 AA;  44576 MW;  03B34684DA0F8255 CRC64;
     MNDLLDPIRG IPVDLELVRR ELDVDLPTAR YLVRTGLITT DGARVLRRGP TTGTCATAAA
     KAAAIRLLEG RTVRTVRVRL PVGTVIGVRI SRVGGDPSEA RVRKPGSDDH VDVTTGVTIA
     ARVEETGSEG VEIRAGRGVG ETPSGKPAIS EAVREQIVDN LRYLVDSYGV GLRVTIEVPD
     GEEIARKTLA HRHGIEGGIS ILGTKGLVDP NSEEAIEGSI RSDLRYVERV PCLVTGYRTM
     DRARRLGIPS RDIVNCHGRY DLALEAVKTG VPADGEVKRF DAVLIFGMPG KLLKLAAGAY
     NTHAKVADAR RESLVTRLVE IGRPDLAVEA ARHEGLISEF LRSLDPDVRR ELFERVCELV
     EERVSSDHDL ECGCALYFRA DDSEEVVEGE GWKRLVRGYD DDLIGRPKG