CBID_SALAI
ID CBID_SALAI Reviewed; 380 AA.
AC A8M4X3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Sare_2704;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
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., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
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; CP000850; ABV98541.1; -; Genomic_DNA.
DR RefSeq; WP_012182842.1; NC_009953.1.
DR AlphaFoldDB; A8M4X3; -.
DR SMR; A8M4X3; -.
DR STRING; 391037.Sare_2704; -.
DR EnsemblBacteria; ABV98541; ABV98541; Sare_2704.
DR GeneID; 5707724; -.
DR KEGG; saq:Sare_2704; -.
DR PATRIC; fig|391037.6.peg.2740; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_11; -.
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.
DR TIGRFAMs; TIGR00312; cbiD; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..380
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_1000083594"
SQ SEQUENCE 380 AA; 38769 MW; D42A71C3178679AF CRC64;
MGYDLPPLRE PDLPRTAKVR PVALRTGWTT GACATAAAKA ALTALVTGVA PAEVEIGLPA
GRRVRFPVAR CDRRDEGAEA VVVKDAGDDP DVTHGAELTA TVGWRPVPGL ALEGGPGVGT
VTKPGLGLAV GGPAINDTPR RMIGEAVAEV VDLTAVGVRV VISVPRGEIM ARKTTNRRLG
IVGGISILGT TGIVRPFSTA SWRASVVQAV QVAAAQGERT VVLCTGGRTE RGARALLPEL
PEVCFVEVGD FTGAAVTAAV THGLSGVAFV GMAGKLAKLA AGVLMTHYTR SKVDLSLLGA
VTAEAGGTAD LATAVTAANT GRHAYELWEA AGLLGPAGDL LCSRVRAVLR RFAGDAVAVD
VAMVDFTGAR VVASSGRWAR
