CBID_GLOVI
ID CBID_GLOVI Reviewed; 357 AA.
AC Q7NK51;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, 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=gll1629;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC89570.1; -; Genomic_DNA.
DR RefSeq; NP_924575.1; NC_005125.1.
DR RefSeq; WP_011141628.1; NC_005125.1.
DR AlphaFoldDB; Q7NK51; -.
DR SMR; Q7NK51; -.
DR STRING; 251221.35212194; -.
DR EnsemblBacteria; BAC89570; BAC89570; BAC89570.
DR KEGG; gvi:gll1629; -.
DR PATRIC; fig|251221.4.peg.1665; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_1_2_3; -.
DR InParanoid; Q7NK51; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR PhylomeDB; Q7NK51; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000000557; 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_0000141667"
SQ SEQUENCE 357 AA; 37549 MW; 0AC13CB48EE364D5 CRC64;
MSRTGYTLPV FAAAAARAAL LHLIEKVPCA SVQLDLLGEQ AAIPIEQVAR LDAETALGVT
RSDPGDNLDL TRHTPVWAWV HLEVGTGEVL RLEAGEGLGR TAAGEAAIYR YARQLMEANV
APLVPTGRTA TVRFILPEGR ALALRTSNAA FGILEGLALL GTSGLSQPLS AADHLESFRA
ALRERAERER RLVFCIGAGG LQAAGRLGLD QGATVQTGNW IGALLVEAGM LGIESVLLLG
YQGKLVKLAA GIFNTSSHVA DGRLETIAAG AVAAGADIET VRTVLEAPTA DAACALLAAA
GWAEKIYAAL AERVSGRSVE YVRKYTERTM AVATMLLDRQ GRVIARDRAA AEWLAEP
