ID A0A929FQ38_9CYAN Unreviewed; 373 AA.
AC A0A929FQ38;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 8.
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=IQ257_07350 {ECO:0000313|EMBL:MBE9148318.1};
OS Coleofasciculus sp. LEGE 07092.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=2777969 {ECO:0000313|EMBL:MBE9148318.1, ECO:0000313|Proteomes:UP000619145};
RN [1] {ECO:0000313|EMBL:MBE9148318.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LEGE 07092 {ECO:0000313|EMBL:MBE9148318.1};
RA Castelo-Branco R., Eusebio N., Adriana R., Vieira A.,
RA Brugerolle De Fraissinette N., Rezende De Castro R., Schneider M.P.,
RA Vasconcelos V., Leao P.N.;
RL Submitted (OCT-2020) 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:MBE9148318.1}.
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DR EMBL; JADEWY010000020; MBE9148318.1; -; Genomic_DNA.
DR RefSeq; WP_193873336.1; NZ_JADEWY010000020.1.
DR Proteomes; UP000619145; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019251; P:anaerobic cobalamin 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:UP000619145};
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 373 AA; 40399 MW; 8B9ADAEF92F66230 CRC64;
MTASQPQSGY TLPVFACAAA IAALRWLRQP QPLNAVSVDL IAPPETVSIP IEQVAGLREG
IALAITRSDP GDNLDLTRNT PIWALVEWGQ PNQCEQVRIL GGEGIGRQMN AGGKAAIYSY
AQRLLQDNLS RLLAAAEKIQ VTFILPAGRQ LAERTSNAAF GVVEGLSLLG TTGISQPLSS
PEQLEAYRQE LQEKASRFNC LVFCVGENGL DLARNLGINP EQLVKTANWL GPLFVTAGLQ
HVPAILLFGY HGKLIKLAGG IFHTHHHLAD GRLEILTAHC AQVGLPTSVL QVIFTSPTTE
VALQYLRQLD IAEGSNWVEQ VYGAIAFAID QRSQDYIRKH SEQSVQVGSV LFDRDRQIVT
TSQIGATLLG QLC
//
