CBID_THEVO
ID CBID_THEVO Reviewed; 378 AA.
AC Q97A63;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=TV0947;
GN ORFNames=TVG0972668;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB60089.1; -; Genomic_DNA.
DR AlphaFoldDB; Q97A63; -.
DR SMR; Q97A63; -.
DR STRING; 273116.14325164; -.
DR EnsemblBacteria; BAB60089; BAB60089; BAB60089.
DR KEGG; tvo:TVG0972668; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_041273_1_0_2; -.
DR OMA; YHGKLIK; -.
DR PhylomeDB; Q97A63; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000001017; 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.
DR TIGRFAMs; TIGR00312; cbiD; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..378
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141702"
SQ SEQUENCE 378 AA; 39916 MW; 035CDD7A35275FE8 CRC64;
MMYASDGSGV NPFQQYGITT GLTAAAAAKA CTLTVLKGVQ NRVVVPTPIG IRIEVKVVES
VRIDESSGYA SAEKFSGDNP DQLNGITIRC HCKVVKKQEN GRSKITISGN AGIGVVEKDG
LGIRPGEKAI SQGARKMIED AVREAAGGYD VELSISVPNG EEFAKLTMNE KVGVFGGISV
LGTTGIEEPV STEEYELHLK YIVAAGRCVS KIIVLCPGNT ALKFAKKYFA LPDKAFVLIG
DKVGAAVSAS IESAYDHVVI FGLPGKLVKI AAGIYNTHSK VADGRMETLA AVAAMYGISK
GAVKRIMESS NTGEAISIIE QEGIVAEVLN TIASRISNRL KADFSRSVGF SVVIIDHDGK
IIGSHLDGHI KEVLKYGK
