CBIT_METVS
ID CBIT_METVS Reviewed; 180 AA.
AC A6UPM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Mevan_0536;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR54443.1; -; Genomic_DNA.
DR RefSeq; WP_011972346.1; NC_009634.1.
DR AlphaFoldDB; A6UPM1; -.
DR SMR; A6UPM1; -.
DR STRING; 406327.Mevan_0536; -.
DR EnsemblBacteria; ABR54443; ABR54443; Mevan_0536.
DR GeneID; 5325897; -.
DR KEGG; mvn:Mevan_0536; -.
DR eggNOG; arCOG00977; Archaea.
DR HOGENOM; CLU_094143_0_0_2; -.
DR OMA; RCKFVYA; -.
DR OrthoDB; 82864at2157; -.
DR UniPathway; UPA00148; UER00229.
DR Proteomes; UP000001107; Chromosome.
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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 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..180
FT /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT (decarboxylating)"
FT /id="PRO_1000046845"
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 180 AA; 20108 MW; 647B5DD597ED6AE7 CRC64;
MIKDSEFYRL DGVPITKEEI RAISVEKLNI CPEDIILDIG CGSGGMTVEI SKRCKFVYAV
DGSKDAIDTT LKNMDKFNVK NCEVYFGDAK DLISNFKVNK AFIGGTQNIE SVIEKLNEKN
VRNIVINTIV LENSVKVIQI LERLNFSIEV ISVLISYGKR ISSGHMMLSK NPITIITAKK
