ID A0A5R9LKE0_9ENTR Unreviewed; 379 AA.
AC A0A5R9LKE0;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 02-APR-2025, entry version 16.
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=FE839_06920 {ECO:0000313|EMBL:TLV21349.1};
OS Klebsiella indica.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
OC Klebsiella.
OX NCBI_TaxID=2582917 {ECO:0000313|EMBL:TLV21349.1, ECO:0000313|Proteomes:UP000307430};
RN [1] {ECO:0000313|EMBL:TLV21349.1, ECO:0000313|Proteomes:UP000307430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TOUT106 {ECO:0000313|EMBL:TLV21349.1,
RC ECO:0000313|Proteomes:UP000307430};
RA Rahi P., Chaudhari D.;
RT "Genome sequence of Klebsiella sp strain TOUT106.";
RL Submitted (MAY-2019) 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:TLV21349.1}.
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DR EMBL; VCHQ01000008; TLV21349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9LKE0; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000307430; Unassembled WGS sequence.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
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:UP000307430};
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 379 AA; 41034 MW; 21B45F1778F696BC CRC64;
MSEQSFDSPV WHNGKALRKG YTTGSCATAA AKVAALMVMR QHLIHQVSII TPSGVTLCLN
VESPHVEGQQ AIAAIRKDGG DDVDATHGML IFARVTLNDS GEITLRGGEG VGTVTRKGIG
LPVGSPAINR TPRHTIESAV REAIGPSRGA EVEIFAPEGE ARAQKTYNSR LGILGGISII
GTTGIVTPMS EESWKRSLSL ELEIKRAAGL DRVVLVPGNH GERFVREQMG IDAQVVVTMS
NFVGYMIEEA VRLGFRQIVL IGHPGKLIKI AAGIFHTHSH IADARMETLV AHLALLGAPL
ELLRQVSECD TTEAAMEHID AYGFHHIYNH LAERICQRVT QMLRFTRTPP TCDAIMFSFD
NNVLGSNRPV AEIARELSC
//
