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Database: UniProt
Entry: A0A161QCM9_9FIRM
LinkDB: A0A161QCM9_9FIRM
Original site: A0A161QCM9_9FIRM 
ID   A0A161QCM9_9FIRM        Unreviewed;       357 AA.
AC   A0A161QCM9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ECO:0000313|EMBL:KYO67028.1};
GN   ORFNames=ATZ99_08450 {ECO:0000313|EMBL:KYO67028.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO67028.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO67028.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO67028.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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:KYO67028.1}.
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DR   EMBL; LOHZ01000023; KYO67028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161QCM9; -.
DR   STRING; 520767.ATZ99_08450; -.
DR   PATRIC; fig|520767.4.peg.935; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000075737; 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:UP000075737};
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   357 AA;  39658 MW;  47665EAF91077562 CRC64;
     MEVIRYGKKM RCGYTTGSCA AAAAKAAVIR LLGGECREVR VRTPSGEVLL IKISECRVEG
     DEAICRVVKD AGDDADATDG IAIYAKVSLR GDGRVLIEGG EGIGRFKENS PYGKKGEAAI
     NKVPRRMIEA SVLEAHPGGA NVLIFAPEGR EIAKKTYNPR MGIEGGISIL GTTGIVYPMS
     EEAYKKVMYT ELEVMRKNTD EAVLTFGNYG MEYIRKAELS KETVKISNFV GEALLYCREL
     GFKKVTLVGH VGKMCKISIG AFNTSSRVVD SRVEAFVYYL AKNGAPRDLI ESVERFKTAE
     ECANFLRESG YDRVLEDMKE GIVRRIKAYL KEDNMKIEVF MYTFKEMQGW GKWSSWE
//
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