CBIT_METTH
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 03-AUG-2022, entry version 133.
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}.
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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 AlphaFoldDB; O26249; -.
DR SMR; O26249; -.
DR STRING; 187420.MTH_146; -.
DR EnsemblBacteria; AAB84652; AAB84652; MTH_146.
DR GeneID; 1470107; -.
DR KEGG; mth:MTH_146; -.
DR HOGENOM; CLU_094143_0_0_2; -.
DR OMA; RCKFVYA; -.
DR BRENDA; 2.1.1.196; 3256.
DR UniPathway; UPA00148; UER00229.
DR EvolutionaryTrace; O26249; -.
DR Proteomes; UP000005223; 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; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 BINDING 17
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786,
FT ECO:0000269|PubMed:12429089"
FT BINDING 41..45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786,
FT ECO:0000269|PubMed:12429089"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786,
FT ECO:0000269|PubMed:12429089"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 124..134
FT /evidence="ECO:0007829|PDB:1L3I"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 155..167
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1L3I"
FT STRAND 179..183
FT /evidence="ECO:0007829|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
