ID   CBID_KLEP3              Reviewed;         379 AA.
AC   B5XUU2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   11-DEC-2019, entry version 62.
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=KPK_0919;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08091.1; -; Genomic_DNA.
DR   SMR; B5XUU2; -.
DR   PRIDE; B5XUU2; -.
DR   EnsemblBacteria; ACI08091; ACI08091; KPK_0919.
DR   KEGG; kpe:KPK_0919; -.
DR   HOGENOM; HOG000009126; -.
DR   KO; K02188; -.
DR   OMA; GGIFHTH; -.
DR   OrthoDB; 1282567at2; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
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..379
FT                   /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT                   /id="PRO_1000133738"
SQ   SEQUENCE   379 AA;  40870 MW;  EDF1B65288F0A855 CRC64;
     MSDQTFDAPV WHHGKALRKG YTTGSCATAA AKVAALMVMR QHLIHQVSIV TPSGVTLCLN
     VESPHVEGQQ AVAAIRKDGG DDVDATHGML IFARVTLNDS GEISLLGGEG IGTVTRKGIG
     LPTGSPAINR TPRHTIETAV REAIGPSRGA QVEIFAPEGV LRAQKTYNAR LGILGGISII
     GTTGIVTPMS EESWKRSLSL ELEIKRAAGL DRVVLVPGNH GERFVREQMG IDPQVVVTMS
     NFVGYMIEEA VRLGFRQIVL IGHPGKLIKI AAGIFHTHSH IADARMETLV AHLALLGAPL
     PLLTLVSECD TTEAAMEHID AWGYQRLYNH LAERICQRVL EMLRFTQHPP ACDAVLFSFD
     NQVLGSSRPL AAIARELTC
//