ID CBIT_METTH STANDARD; PRT; 192 AA. AC O26249; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 07-MAR-2006, entry version 37. DE Probable cobalt-precorrin-6Y C(15)-methyltransferase [decarboxylating] DE (EC 2.1.1.-). GN Name=cbiT; OrderedLocusNames=MTH146; 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). 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: Adenosylcobalamin biosynthesis; anaerobic branch of CC corrin ring synthesis; tenth step. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archeal- CC 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 PDB; 1F38; X-ray; A/B/C/D=1-192. DR PDB; 1KXZ; X-ray; A/B/C/D/E/F/G/H=1-192. DR PDB; 1L3B; X-ray; A/B/C/D/E/F/G/H=1-192. DR PDB; 1L3C; X-ray; A/B/C/D=1-192. DR PDB; 1L3I; X-ray; A/B/C/D/E/F=1-192. DR GenomeReviews; AE000666_GR; MTH146. DR BioCyc; MTHE187420:MTH146-MONOMER; -. DR LinkHub; O26249; -. DR HAMAP; MF_00786; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR012376; Precrr_mtas_CbiT. DR InterPro; IPR000051; SAM_bd. DR Pfam; PF08241; Methyltransf_11; 1. DR Pfam; PF01170; UPF0020; 1. DR PIRSF; PIRSF019019; Precrr_mtas_CbiT; 1. KW 3D-structure; Cobalamin biosynthesis; Complete proteome; KW Methyltransferase; Transferase. FT CHAIN 1 192 Probable cobalt-precorrin-6Y C(15)- FT methyltransferase [decarboxylating]. FT /FTId=PRO_0000134941. FT HELIX 4 6 FT STRAND 7 7 FT TURN 11 12 FT STRAND 13 13 FT HELIX 19 29 FT TURN 33 34 FT STRAND 36 41 FT TURN 43 44 FT STRAND 45 45 FT HELIX 46 52 FT TURN 53 54 FT STRAND 55 63 FT HELIX 65 77 FT TURN 78 79 FT TURN 82 83 FT STRAND 84 89 FT HELIX 91 95 FT TURN 96 97 FT STRAND 98 98 FT STRAND 101 107 FT TURN 110 111 FT HELIX 113 122 FT TURN 123 123 FT STRAND 124 134 FT STRAND 136 136 FT HELIX 137 149 FT TURN 150 151 FT STRAND 155 167 FT TURN 168 169 FT STRAND 170 175 FT STRAND 179 183 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 //