CBID_METC4
ID CBID_METC4 Reviewed; 361 AA.
AC Q9X7G7; B7L3N5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Mchl_5729;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OG Plasmid pMCHL01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10200311; DOI=10.1073/pnas.96.8.4615;
RA Vannelli T., Messmer M., Studer A., Vuilleumier S., Leisinger T.;
RT "A corrinoid-dependent catabolic pathway for growth of a Methylobacterium
RT strain with chloromethane.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4615-4620(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of plasmid1 of Methylobacterium chloromethanicum CM4.";
RL Submitted (DEC-2008) 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; AJ011317; CAB40740.1; -; Genomic_DNA.
DR EMBL; CP001299; ACK86443.1; -; Genomic_DNA.
DR RefSeq; WP_012606333.1; NC_011758.1.
DR AlphaFoldDB; Q9X7G7; -.
DR SMR; Q9X7G7; -.
DR EnsemblBacteria; ACK86443; ACK86443; Mchl_5729.
DR KEGG; mch:Mchl_5729; -.
DR HOGENOM; CLU_041273_0_0_5; -.
DR OMA; YHGKLIK; -.
DR BioCyc; MEXT440085:MCHL_RS27865-MON; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002385; Plasmid pCMU01.
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; Plasmid;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..361
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141673"
SQ SEQUENCE 361 AA; 37534 MW; 4913FE8B70B3B3F2 CRC64;
MNSETGALRR GWTTGTCASA AARAAFEALL GIEPEDPVPV TLPSGARPTF ALARLDRGSG
FVRAGIVKDA GDDPDVTHGA LVLATLRFGA PATGIVFRAG PGVGIVTKPG LPLPPGEPAI
NAMPRRMIRT ALTEVAEANG VTCDLVVEVG IEDGERIAER TMNRRLGIIG GLSILGTTGV
VVPYSCAAWI ASIHRGIDVA RAEGLTHLAG ATGATSEAAI RNLYGLPEQA LIDMGDFVGG
MLKYIRGHPV ARVTIAGGFA KMTKLAQGRL DLHSKREAID FRWLAELYCS IGGKAESGMS
VRTANTALEV LQMAQAEHVP IAPAIARSAC RVAAGALARA DIALDVAIFD RDGCLIASER
C