ID CBIT_METTH Reviewed; 192 AA. AC O26249; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 12-AUG-2020, entry version 126. 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=MTH_146; OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H; RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997; RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., RA Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: RT functional analysis and comparative genomics."; RL J. Bacteriol. 179:7135-7155(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, SUBUNIT, AND FUNCTION. RX PubMed=12429089; DOI=10.1016/s0969-2126(02)00876-6; RA Keller J.P., Smith P.M., Benach J., Christendat D., deTitta G.T., RA Hunt J.F.; RT "The crystal structure of MT0146/CbiT suggests that the putative precorrin- RT 8w decarboxylase is a methyltransferase."; RL Structure 10:1475-1487(2002). 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:0000305|PubMed:12429089}. 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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12429089}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type CC CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- CAUTION: Was originally thought to be a precorrin-8w decarboxylase. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000666; AAB84652.1; -; Genomic_DNA. DR PIR; D69061; D69061. DR RefSeq; WP_010875785.1; NC_000916.1. DR PDB; 1F38; X-ray; 2.40 A; A/B/C/D=1-192. DR PDB; 1KXZ; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-192. DR PDB; 1L3B; X-ray; 2.65 A; A/B/C/D/E/F/G/H=1-192. DR PDB; 1L3C; X-ray; 2.31 A; A/B/C/D=1-192. DR PDB; 1L3I; X-ray; 1.95 A; A/B/C/D/E/F=1-192. DR PDBsum; 1F38; -. DR PDBsum; 1KXZ; -. DR PDBsum; 1L3B; -. DR PDBsum; 1L3C; -. DR PDBsum; 1L3I; -. DR SMR; O26249; -. DR PRIDE; O26249; -. DR EnsemblBacteria; AAB84652; AAB84652; MTH_146. DR GeneID; 1470107; -. DR KEGG; mth:MTH_146; -. DR HOGENOM; CLU_094143_0_0_2; -. DR KO; K02191; -. DR OMA; RCKFVYA; -. DR BioCyc; MTHE187420:G1G16-133-MONOMER; -. DR BRENDA; 2.1.1.289; 3256. DR UniPathway; UPA00148; UER00229. DR EvolutionaryTrace; O26249; -. DR Proteomes; UP000005223; Chromosome. 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 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. DR Pfam; PF13847; Methyltransf_31; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02469; CbiT; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..192 FT /note="Probable cobalt-precorrin-6B C(15)-methyltransferase FT (decarboxylating)" FT /id="PRO_0000134941" FT REGION 41..45 FT /note="S-adenosyl-L-methionine binding" FT BINDING 17 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786, FT ECO:0000269|PubMed:12429089" FT BINDING 62 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786, FT ECO:0000269|PubMed:12429089" FT BINDING 91 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786, FT ECO:0000269|PubMed:12429089" FT HELIX 4..6 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 19..29 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 36..41 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 46..52 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 55..63 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 65..77 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 84..89 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 91..95 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 101..107 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 113..122 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 124..134 FT /evidence="ECO:0000244|PDB:1L3I" FT HELIX 137..149 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 155..167 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 170..175 FT /evidence="ECO:0000244|PDB:1L3I" FT STRAND 179..183 FT /evidence="ECO:0000244|PDB:1L3I" SQ SEQUENCE 192 AA; 20714 MW; 7BFA35D8BD3C3982 CRC64; MIPDDEFIKN PSVPGPTAME VRCLIMCLAE PGKNDVAVDV GCGTGGVTLE LAGRVRRVYA IDRNPEAIST TEMNLQRHGL GDNVTLMEGD APEALCKIPD IDIAVVGGSG GELQEILRII KDKLKPGGRI IVTAILLETK FEAMECLRDL GFDVNITELN IARGRALDRG TMMVSRNPVA LIYTGVSHEN KD //