CBID_METMA
ID CBID_METMA Reviewed; 339 AA.
AC Q8PWA9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=MM_1681;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31377.1; -; Genomic_DNA.
DR RefSeq; WP_011033623.1; NC_003901.1.
DR AlphaFoldDB; Q8PWA9; -.
DR SMR; Q8PWA9; -.
DR STRING; 192952.MM_1681; -.
DR EnsemblBacteria; AAM31377; AAM31377; MM_1681.
DR GeneID; 24878421; -.
DR GeneID; 66136831; -.
DR KEGG; mma:MM_1681; -.
DR PATRIC; fig|192952.21.peg.1948; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_820433_0_0_2; -.
DR OMA; NDHESDI; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000000595; 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 PIRSF; PIRSF026782; 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..339
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141694"
SQ SEQUENCE 339 AA; 36315 MW; 7721F2D67EEB32E8 CRC64;
MIDPVNNFKI PEEWIALTGL PREELEKNVA SGMVVVLSDG SVLKRGYTTG TTASAAAKAA
VLSLKKKIDS VSVPTPVGLR AHLEVSESSP GRAVVKKILN DHESDITRGL EFVGEAREAE
GIHVLGGKGI GVVRRDGLQV PKGKPAINPK PMEQIRAAVK EAVEELGLQG AEVTISIPEG
ERIGKETLNS RIGVEGGISV LGSTGFVEPW NDHLGETRGD LIRCTDKVVL TTGRIGMRYS
HMLFPEYTVV MVGSRISEGL DYASGDIIIC GLPGLVLKWG NPEMLEGSGY ATVVEMLEKA
PQHERLKEAF EMAVEKGKGA RIVVIDRDGS VLMDSKSES
