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 24-NOV-2009, entry version 67. DE RecName: Full=Probable cobalt-precorrin-6Y C(15)-methyltransferase [decarboxylating]; DE EC=2.1.1.-; GN Name=cbiT; OrderedLocusNames=MTH_146; OS Methanobacterium thermoautotrophicum. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Delta H; RX MEDLINE=98037514; 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 MEDLINE=22317553; 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: Probably catalyzes the methylation of either C-15 or C-5 CC in cobalt-precorrin-6Y to form cobalt-precorrin-7W. Methylation of CC C-15 would probably be followed by a spontaneous decarboxylation CC of C-12. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 8/10. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC Archaeal-type cbiT family. CC -!- CAUTION: Was originally thought to be a precorrin-8w CC decarboxylase. 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; NP_275289.1; -. 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 STRING; O26249; -. DR GeneID; 1470107; -. DR GenomeReviews; AE000666_GR; MTH_146. DR KEGG; mth:MTH146; -. DR NMPDR; fig|187420.1.peg.144; -. DR HOGENOM; O26249; -. DR OMA; EFIRGNC; -. DR BioCyc; MTHE187420:MTH146-MON; -. DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:HAMAP. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046140; P:corrin biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00786; -; 1. DR InterPro; IPR014008; Cbl_synth_CbiT_core. DR InterPro; IPR013216; Methyltransf_11. DR Pfam; PF08241; Methyltransf_11; 1. DR TIGRFAMs; TIGR02469; CbiT; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Complete proteome; KW Methyltransferase; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 192 Probable cobalt-precorrin-6Y 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 BINDING 62 62 S-adenosyl-L-methionine. FT BINDING 91 91 S-adenosyl-L-methionine; via amide FT nitrogen. FT HELIX 4 6 FT HELIX 19 29 FT STRAND 36 41 FT HELIX 46 52 FT STRAND 55 63 FT HELIX 65 77 FT STRAND 84 89 FT HELIX 91 95 FT STRAND 101 106 FT HELIX 113 122 FT STRAND 124 134 FT HELIX 137 149 FT STRAND 154 166 FT STRAND 171 175 FT STRAND 179 184 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 //