CBIT_METM6
ID CBIT_METM6 Reviewed; 181 AA.
AC A9AA91;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00786};
DE EC=2.1.1.196 {ECO:0000255|HAMAP-Rule:MF_00786};
GN Name=cbiT {ECO:0000255|HAMAP-Rule:MF_00786}; OrderedLocusNames=MmarC6_1451;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00786}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}.
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DR EMBL; CP000867; ABX02264.1; -; Genomic_DNA.
DR RefSeq; WP_012194184.1; NC_009975.1.
DR AlphaFoldDB; A9AA91; -.
DR SMR; A9AA91; -.
DR STRING; 444158.MmarC6_1451; -.
DR EnsemblBacteria; ABX02264; ABX02264; MmarC6_1451.
DR GeneID; 5737457; -.
DR KEGG; mmx:MmarC6_1451; -.
DR eggNOG; arCOG00977; Archaea.
DR HOGENOM; CLU_094143_0_0_2; -.
DR OMA; RCKFVYA; -.
DR OrthoDB; 82864at2157; -.
DR PhylomeDB; A9AA91; -.
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 Gene3D; 3.40.50.150; -; 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 Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02469; CbiT; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..181
FT /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT (decarboxylating)"
FT /id="PRO_1000133725"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 40..44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
SQ SEQUENCE 181 AA; 20099 MW; D4B560227C1EC4A4 CRC64;
MIQDSEFFRM EGVPITKEEI RAVSIGKLNL DPEDIVLDIG CGSGGMSVEI AKRSKFVYSI
DNSEDAKNTT SINLKKFKIE NCEVFLGDAK DLISKFDFNK VFIGGTQNIE QILEILKEKK
VEKVVANTIV LENGVKIISK FEELGYNVDF VNVSVSYGKK ISSGHIMLSK NPITIITATL
K