CBID_NOSS1
ID CBID_NOSS1 Reviewed; 370 AA.
AC Q8YT79;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=all2847;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000019; BAB74546.1; -; Genomic_DNA.
DR PIR; AH2161; AH2161.
DR RefSeq; WP_010996998.1; NZ_RSCN01000003.1.
DR AlphaFoldDB; Q8YT79; -.
DR SMR; Q8YT79; -.
DR STRING; 103690.17131941; -.
DR EnsemblBacteria; BAB74546; BAB74546; BAB74546.
DR KEGG; ana:all2847; -.
DR eggNOG; COG1903; Bacteria.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000002483; 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..370
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141656"
SQ SEQUENCE 370 AA; 39843 MW; 01B229CB24417ECB CRC64;
MRSGYTLPVF ACAGAIAALH WLRQRQSIQV ALVDLIEPAQ IAEVPIEQVA GLSANMALAI
TRSDPGDNLD LTKNTPIWAV VEWGKTGGEQ VTIKGGEGIG KQVNADNQAA IYSYAQRLLQ
ANLTRLLAPE ESIIVTIILP EGRSLAVRTS NSAFGVVEGL SLLGTTGISQ PLSSPDQLDA
FRSELQHKAS LYESLVFCIG ENGLDLARKI GINAEKLVKT ANWLGPMLVE ADALGVKEIL
LFGYHGKLMK LAGGIFHTHH HLADGRREVL ATHCALAGLS KQDIEIVFHS PTAEAALKHL
KALDISTGND WVNQVYSAIA ETIDSRCQEY MQSHSSRGTA ATICGSILFD RDRKIIVKSK
TACNLMGNLC
