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Database: UniProt
Entry: A0A3N6IJ44_9ACTN
LinkDB: A0A3N6IJ44_9ACTN
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ID   A0A3N6IJ44_9ACTN        Unreviewed;       372 AA.
AC   A0A3N6IJ44;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00787};
DE            EC=2.1.1.195 {ECO:0000256|HAMAP-Rule:MF_00787};
DE   AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000256|HAMAP-Rule:MF_00787};
GN   Name=cbiD {ECO:0000256|HAMAP-Rule:MF_00787};
GN   ORFNames=EES45_16770 {ECO:0000313|EMBL:RPK78725.1};
OS   Streptomyces sp. ADI97-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK78725.1, ECO:0000313|Proteomes:UP000281409};
RN   [1] {ECO:0000313|EMBL:RPK78725.1, ECO:0000313|Proteomes:UP000281409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK78725.1,
RC   ECO:0000313|Proteomes:UP000281409};
RA   Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA   Busche T., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT   secondary metabolite biosynthesis gene clusters and some of their
RT   products.";
RL   Submitted (NOV-2018) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00787}.
CC   -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00787}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RPK78725.1}.
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DR   EMBL; RPGY01000088; RPK78725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6IJ44; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000281409; Unassembled WGS sequence.
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; CbiD-like; 1.
DR   HAMAP; MF_00787; CbiD; 1.
DR   InterPro; IPR002748; CbiD.
DR   InterPro; IPR036074; CbiD_sf.
DR   NCBIfam; TIGR00312; cbiD; 1.
DR   PANTHER; PTHR35863; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR35863:SF1; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR   Pfam; PF01888; CbiD; 1.
DR   PIRSF; PIRSF026782; CbiD; 1.
DR   SUPFAM; SSF111342; CbiD-like; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00787};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00787}; Reference proteome {ECO:0000313|Proteomes:UP000281409};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00787};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00787}.
SQ   SEQUENCE   372 AA;  38083 MW;  A1D636C5C29F1A35 CRC64;
     MSSEAQGGRT AQLKHTGLRP GWTTGACATA ATTAAYTALL TGEFPDPVTI TLPRGQTPAF
     ALAVEELAEG RATAGVVKDA GDDPDVTHGA LVRSTVRLLP PGSGVVFRAG PGVGTVTLPG
     LPLDVGEPAI NPVPRQMMRD HVARVAAEHG GTGDVEITIS VDDGEEIARF TWNIRLGILG
     GLSILGTTGV VVPYSCSAWI DSIRRGVDVA LAAGQTHVAG CTGSTSEKTV AAEHGLPEIA
     LLDMGDFAGA VLKYVRRHPV DRLTICGGFA KLSKLAAGHL DLHSGRSQVD KPFLARLARQ
     GGASEALAAE IEVANTGLAA LQLCMAAGVP LGDLVAVAAR DQALSVLRGA PVAVDVICID
     RAGTVVGRSE VR
//
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