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 05-OCT-2016, entry version 111. 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}; GN OrderedLocusNames=MTH_146; OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / OS JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium OS thermoautotrophicum). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC 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; 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., RA Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., RA Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., RA Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., RA McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., RA Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum RT deltaH: 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 RT precorrin-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- CC 7. {ECO:0000305|PubMed:12429089}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-6B + S-adenosyl-L-methionine CC = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12429089}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC Archaeal-type CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- CAUTION: Was originally thought to be a precorrin-8w CC decarboxylase. {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 ProteinModelPortal; O26249; -. DR STRING; 187420.MTH146; -. DR PRIDE; O26249; -. DR EnsemblBacteria; AAB84652; AAB84652; MTH_146. DR GeneID; 1470107; -. DR KEGG; mth:MTH_146; -. DR eggNOG; arCOG00977; Archaea. DR eggNOG; COG2242; LUCA. DR KO; K02191; -. DR OMA; KFVYAID; -. DR BioCyc; MTHE187420:GJNM-146-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-HAMAP. 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. 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; Complete proteome; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 192 Probable cobalt-precorrin-6B C(15)- FT methyltransferase (decarboxylating). FT /FTId=PRO_0000134941. FT REGION 41 45 S-adenosyl-L-methionine binding. FT BINDING 17 17 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00786, FT ECO:0000269|PubMed:12429089}. FT BINDING 62 62 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00786, FT ECO:0000269|PubMed:12429089}. FT BINDING 91 91 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00786, FT ECO:0000269|PubMed:12429089}. FT HELIX 4 6 {ECO:0000244|PDB:1L3I}. FT HELIX 19 29 {ECO:0000244|PDB:1L3I}. FT STRAND 36 41 {ECO:0000244|PDB:1L3I}. FT HELIX 46 52 {ECO:0000244|PDB:1L3I}. FT STRAND 55 63 {ECO:0000244|PDB:1L3I}. FT HELIX 65 77 {ECO:0000244|PDB:1L3I}. FT STRAND 84 89 {ECO:0000244|PDB:1L3I}. FT HELIX 91 95 {ECO:0000244|PDB:1L3I}. FT STRAND 101 107 {ECO:0000244|PDB:1L3I}. FT HELIX 113 122 {ECO:0000244|PDB:1L3I}. FT STRAND 124 134 {ECO:0000244|PDB:1L3I}. FT HELIX 137 149 {ECO:0000244|PDB:1L3I}. FT STRAND 155 167 {ECO:0000244|PDB:1L3I}. FT STRAND 170 175 {ECO:0000244|PDB:1L3I}. FT STRAND 179 183 {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 //