CBID_THET2
ID CBID_THET2 Reviewed; 366 AA.
AC P61989;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=TT_P0008;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017222; AAS82338.1; -; Genomic_DNA.
DR RefSeq; WP_008631402.1; NC_005838.1.
DR AlphaFoldDB; P61989; -.
DR SMR; P61989; -.
DR STRING; 262724.TT_P0008; -.
DR PRIDE; P61989; -.
DR EnsemblBacteria; AAS82338; AAS82338; TT_P0008.
DR GeneID; 3167863; -.
DR KEGG; tth:TT_P0008; -.
DR eggNOG; COG1903; Bacteria.
DR HOGENOM; CLU_041273_0_0_0; -.
DR OMA; YHGKLIK; -.
DR OrthoDB; 1282567at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000000592; Plasmid pTT27.
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; Plasmid;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..366
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141688"
SQ SEQUENCE 366 AA; 38946 MW; F4C115E4EA2A3444 CRC64;
MSHPYPPPRD KKGSRIGFTT GANAAAAAKA AALALLGEAP EVVDIWLPAG WRQPFRVFRL
ERKGDGVLVG MIKDAGDDPD VTHGAEIQAF VRFASEDRLE GGEGVGVVTK PGLGVPVGEP
AINPVPRRMI WEAVREVTER PLAVTIAIPG GEELAKKTLN PRLGILGGLS VLGTTGVVKP
YSTSAFRMSV VQAVGVARAN GLLEIAATTG GKSERFAQRL LPHLPEMAFI EMGDFVGDVL
RAARKVGVEV VRVVGMIGKI SKMADGKTMT HAAGGEVNLS LLLSLLKEAG ASPKALKEAE
GAATARRFLE IALEEGLELF FVNLVRLAQE KLQAYIGERP FVSVALTDFD EGRCLAAWPD
REVYRG
