CBID_METHJ
ID CBID_METHJ Reviewed; 335 AA.
AC Q2FRR2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=Mhun_3215;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC EC=2.1.1.195; Evidence={ECO:0000255|HAMAP-Rule:MF_00787};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP-
CC Rule:MF_00787}.
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DR EMBL; CP000254; ABD42897.1; -; Genomic_DNA.
DR RefSeq; WP_011450142.1; NC_007796.1.
DR AlphaFoldDB; Q2FRR2; -.
DR SMR; Q2FRR2; -.
DR STRING; 323259.Mhun_3215; -.
DR EnsemblBacteria; ABD42897; ABD42897; Mhun_3215.
DR GeneID; 3922268; -.
DR KEGG; mhu:Mhun_3215; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_820433_0_0_2; -.
DR OMA; NDHESDI; -.
DR OrthoDB; 57676at2157; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
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 Gene3D; 3.30.2110.10; -; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR PANTHER; PTHR35863; PTHR35863; 1.
DR Pfam; PF01888; CbiD; 1.
DR SUPFAM; SSF111342; SSF111342; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..335
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000257787"
SQ SEQUENCE 335 AA; 36021 MW; 461407B1B486C8E9 CRC64;
MQDPVSGFIY PEEWISLCTD ETERLLVSQG LAVLTSDGTI RRRGFTTGSS ASAAAKASVL
SLTKTGFDEV SILTPAGIRV QIPVTIARGT GECRKYSGDY PGDVTAGLVF TAEATPADSG
TTLVFGEGIG RWSRDTPRYK TGDPAVSCQA MDEIKNAIEE AVQETGIPGV SVRIFAREGR
IVAEKTLNQM VGVVGGISVL GTTGFVEPWD DHLEQTVCDR AVHAERVVLT TGRIGMRYAR
MLFPDHEVIL AGSRLGTIIP HLTGEVIICG LPALVLKYIN PVILEGTGFS TVEEFMTNDR
FLPAMQTSFQ IYKSAHPNVR IVVVNREGAI IGDSQ