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Database: UniProt
Entry: B3T966_9ARCH
LinkDB: B3T966_9ARCH
Original site: B3T966_9ARCH 
ID   B3T966_9ARCH            Unreviewed;       196 AA.
AC   B3T966;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00786};
DE            EC=2.1.1.196 {ECO:0000256|HAMAP-Rule:MF_00786};
GN   Name=cbiT {ECO:0000256|HAMAP-Rule:MF_00786};
GN   ORFNames=ALOHA_HF4000APKG6D9ctg2g31 {ECO:0000313|EMBL:ABZ09125.1};
OS   uncultured marine crenarchaeote HF4000_APKG6D9.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   environmental samples.
OX   NCBI_TaxID=455597 {ECO:0000313|EMBL:ABZ09125.1};
RN   [1] {ECO:0000313|EMBL:ABZ09125.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA   Konstantinidis K.T., Delong E.F.;
RT   "Genomic patterns of recombination, clonal divergence and environment in
RT   marine microbial populations.";
RL   ISME J. 2:1052-1065(2008).
CC   -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B
CC       followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
CC       {ECO:0000256|HAMAP-Rule:MF_00786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC         CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00786};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 8/10. {ECO:0000256|HAMAP-Rule:MF_00786}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC       CbiT family. {ECO:0000256|HAMAP-Rule:MF_00786}.
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DR   EMBL; EU016644; ABZ09125.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3T966; -.
DR   UniPathway; UPA00148; UER00229.
DR   GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00786; CbiT; 1.
DR   InterPro; IPR023475; CbiT.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR02469; CbiT; 1.
DR   PANTHER; PTHR43182; COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR43182:SF1; COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00786};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00786};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00786};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00786}.
FT   DOMAIN          38..158
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
FT   BINDING         23
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT   BINDING         47..51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT   BINDING         99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
SQ   SEQUENCE   196 AA;  21443 MW;  8BC43687351EDCC6 CRC64;
     MWNFKTPGIP DENFERADKV PITKEEVRTI QISKARLKQG QTVYDIGCGS GSISVEAALQ
     VESSGKILAI DFDEKAIELT KKNAEKFQIS NITTIFGNAK EKILELEQAD VIFIGGTGGD
     TQKIVELSQE KLKSGGRIVI GTILIETLSA VLQILEKLQF KDVDITQVTI SKSRKTSTGT
     MMLARNPVTI ISATKI
//
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