CBID_MARMS
ID CBID_MARMS Reviewed; 384 AA.
AC A6W0Q2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Mmwyl1_3378;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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; CP000749; ABR72281.1; -; Genomic_DNA.
DR RefSeq; WP_012071048.1; NC_009654.1.
DR AlphaFoldDB; A6W0Q2; -.
DR SMR; A6W0Q2; -.
DR STRING; 400668.Mmwyl1_3378; -.
DR EnsemblBacteria; ABR72281; ABR72281; Mmwyl1_3378.
DR KEGG; mmw:Mmwyl1_3378; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_6; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
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.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..384
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000083592"
SQ SEQUENCE 384 AA; 40552 MW; AFA117B9AF7E65D9 CRC64;
MWPESAESPA PLRTGLTTGT CATACCVAAA QALFADQQAA SVSVTLPKGK VVDLPIIEYQ
TIDAGMKTST IKDAGDDPDA THGATLFVEL RLSPEQGVRF RAAQGVGIVT RTGLLLDVGE
PAINPVPRKM MTEHLKGFAQ TYHYQGGFDV SVGVINGEQI AQKTMNPRLG ILGGLSILGT
TGIVRPFSCA AYIASIHQGI DVARANGLTH IAATTGNASE DAIKSHYQLD DMALIEMGDF
VGAVLKHIKK VEQADFAKLN SSTQLQTLSI CGGFGKISKL AQHHMDLNSR ASSIDLGALA
KLAASLGADN ALQERMTKAN TSVEALSFAI SDGLPLADAI CQQALDFARQ YIPAHIALEV
WAIDRKGQFV GKALDADNSK RDEP
