CBID_META3
ID CBID_META3 Reviewed; 378 AA.
AC A6UT10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Maeo_0040;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
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; CP000743; ABR55632.1; -; Genomic_DNA.
DR RefSeq; WP_011972764.1; NC_009635.1.
DR AlphaFoldDB; A6UT10; -.
DR SMR; A6UT10; -.
DR STRING; 419665.Maeo_0040; -.
DR EnsemblBacteria; ABR55632; ABR55632; Maeo_0040.
DR GeneID; 5327512; -.
DR KEGG; mae:Maeo_0040; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_041273_1_0_2; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 57676at2157; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001106; 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..378
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000046862"
SQ SEQUENCE 378 AA; 41990 MW; A5F87926815C7BC0 CRC64;
MIYDFLKEKK FGYTTGSCVV AGAYCGIYYL KHSVKLNIVE LENSKNDKLI IPIEDVKLGK
IATIKNINNT GKIKPNRATT IVKKFSGEDI DITNGIDIVV DVELLKMEKD KPKIEIVGGN
GVGIVTKDGL QIKKGEYAIN PKPREMIKNN IINLLDDDER AIIKITIPKG EELAKKTLNP
KLGIIGGISI LGTTGIVRPM SNEAYKESLA PQIDVALANN YKKLIFTPGN IGTKYAKIKY
GVDDDNIVEV SNFWSFMLDK AVEKGVKDIL IFGHSGKIIK LAGGIYDTHS KVADARNEIL
TAYSSPFIND KQILKNILYS NTTEEIVKIL EKENILHEVF NLIAERVVER VSSRWEGIKF
SCVIIDMKGD ILGSHIYS