CBID_ALKOO
ID CBID_ALKOO Reviewed; 357 AA.
AC A8MG25;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Clos_1016;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-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; CP000853; ABW18563.1; -; Genomic_DNA.
DR AlphaFoldDB; A8MG25; -.
DR SMR; A8MG25; -.
DR STRING; 350688.Clos_1016; -.
DR EnsemblBacteria; ABW18563; ABW18563; Clos_1016.
DR KEGG; aoe:Clos_1016; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_0_9; -.
DR OMA; YHGKLIK; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000000269; 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..357
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000062245"
SQ SEQUENCE 357 AA; 38908 MW; 0756E01DD4DD98D7 CRC64;
MLDLYVIKEG KRLRCGYTTG SCAAAAAKAA AIMLETGKVL QFVEIDTPAN IPLKLEVHNP
SIDPEKASCA IVKDAGDDPD NTDGIEIYAE VRKRQDGQVH IHGGTGIGRI VRKGLFGTVG
QAAINPVPLQ MIEKEIRAVS DKGYDVTIYA PQGEVIAKKT FNANIGIEGG ISIIGTKGIV
YPMSEEALIK TIYMEMDMVE QKHGLSNIIL VPGNYGEKIS DTLGLSEARV KISNYIGDSL
LYAYNKGFQS MTLIGHIGKF SKLSIGVFNT HSKVCDGRME AFIYYLALMG APRQLIEEVN
GAVTAEEGLH ICIDAGYGEV IKKMEQGAEQ KIRKYIKDEN YPVKVIIYSM ERGVHMG
