ID F3KM74_9ARCH Unreviewed; 195 AA.
AC F3KM74;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 ORFNames=Nlim_1604 {ECO:0000313|EMBL:EGG41593.1};
OS Candidatus Nitrosarchaeum limnium SFB1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=886738 {ECO:0000313|EMBL:EGG41593.1};
RN [1] {ECO:0000313|EMBL:EGG41593.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB1 {ECO:0000313|EMBL:EGG41593.1};
RX PubMed=21364937; DOI=10.1371/journal.pone.0016626;
RA Blainey P.C., Mosier A.C., Potanina A., Francis C.A., Quake S.R.;
RT "Genome of a low-salinity ammonia-oxidizing archaeon determined by single-
RT cell and metagenomic analysis.";
RL PLoS ONE 6:E16626-E16626(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGG41593.1}.
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DR EMBL; AEGP01000051; EGG41593.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KM74; -.
DR STRING; 886738.Nlim_1604; -.
DR PATRIC; fig|886738.10.peg.1745; -.
DR HOGENOM; CLU_094143_0_0_2; -.
DR UniPathway; UPA00148; UER00229.
DR Proteomes; UP000004348; 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};
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 41..139
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 47..51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00786"
SQ SEQUENCE 195 AA; 21487 MW; A4E7C1032DA02E06 CRC64;
MWNFKTPGIP DEFFERTENV PITKEEVRTI QISKARLCPG HIVYDIGCGS GSISVEAAIQ
IETGKVIAID YDENAIELTK KNIAKFDLKN ILVILGNAKE KILELEQADA IFIGGTGGDT
EEIVKLCQNK LKSGGRIVVG IILIETLYSV LRVFEKLEFD SVDITQVTIS KSRKTSKGTM
MLARNPVTII SATKI
//
