CBID_RUBXD
ID CBID_RUBXD Reviewed; 388 AA.
AC Q1AYB7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Rxyl_0641;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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; CP000386; ABG03611.1; -; Genomic_DNA.
DR RefSeq; WP_011563629.1; NC_008148.1.
DR AlphaFoldDB; Q1AYB7; -.
DR SMR; Q1AYB7; -.
DR STRING; 266117.Rxyl_0641; -.
DR EnsemblBacteria; ABG03611; ABG03611; Rxyl_0641.
DR KEGG; rxy:Rxyl_0641; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_11; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR PhylomeDB; Q1AYB7; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000006637; 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..388
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257776"
SQ SEQUENCE 388 AA; 41209 MW; 0A31B310F16238E8 CRC64;
MPERRELREP PMPPSMARVR GRKLRTGWTT GTCAAAAAKA AARALASGEA QEMVEVRLPG
RGEGRRVRFG VERCELGEGW AEAVVVKDAG DDPDVTHGAH LTARVSWREE PGVELDRGEG
VGVVTKPGLG LPVGAPAINP VPRRMILYSL EEALDTRRRG VRVVISVPGG EEMARKTTNP
RLGIVGGISI LGTTGIVRPF STAAWAASVV QAIDVVAAQG GDTFVLSTGG LTERAAMRLL
PHLEEVCFIE VGDFTGQAVR RAAKRGLGRG FFVGMAGKLA KLASGVMMTH WTRSRVDTSL
LAEITRKAGG SERLAEEVEG ANSARHAYEL WRAAGLSGAP RLLCARVAEN LREHAGGALE
MHAIMVDFDT LEPVGASPGA LELTAWRG
