ID Q2NI10_METST Unreviewed; 191 AA.
AC Q2NI10;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00786};
DE EC=2.1.1.196 {ECO:0000256|HAMAP-Rule:MF_00786};
GN Name=cbiT {ECO:0000256|HAMAP-Rule:MF_00786,
GN ECO:0000313|EMBL:ABC56506.1};
GN OrderedLocusNames=Msp_0087 {ECO:0000313|EMBL:ABC56506.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC56506.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC56506.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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:0000256|HAMAP-Rule:MF_00786}.
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:0000256|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:0000256|HAMAP-Rule:MF_00786}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC CbiT family. {ECO:0000256|HAMAP-Rule:MF_00786}.
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DR EMBL; CP000102; ABC56506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NI10; -.
DR STRING; 339860.Msp_0087; -.
DR KEGG; mst:Msp_0087; -.
DR eggNOG; arCOG00977; Archaea.
DR HOGENOM; CLU_094143_0_0_2; -.
DR UniPathway; UPA00148; UER00229.
DR Proteomes; UP000001931; 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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR02469; CbiT; 1.
DR PANTHER; PTHR43182; COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING); 1.
DR PANTHER; PTHR43182:SF1; COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00786};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00786}; Reference proteome {ECO:0000313|Proteomes:UP000001931};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00786};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00786}.
FT DOMAIN 37..149
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 45..49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
SQ SEQUENCE 191 AA; 20827 MW; 1B5B5E6710600F93 CRC64;
MYFDITPNNE FIKTEKVPGP TKEEIRALVI SKVKLTDEDV VVDVGCGTGG LTLEFAKRAK
KIYSIDMNPD AIKTTRANLE KFGLQNKVEL IEDEGLKALD HIEDFTKLMI GGSGGNLDNI
IETGYLKLPI GGRIVITSIV LETATDSVHM LKELGAEPEV VNISVSKGTL LDRGVMMKAL
NPITIVSARK I
//
