CBID_ARCFU
ID CBID_ARCFU Reviewed; 298 AA.
AC O29535;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=AF_0723;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90519.1; -; Genomic_DNA.
DR PIR; C69340; C69340.
DR RefSeq; WP_010878226.1; NC_000917.1.
DR PDB; 1SR8; X-ray; 1.90 A; A=1-298.
DR PDBsum; 1SR8; -.
DR AlphaFoldDB; O29535; -.
DR SMR; O29535; -.
DR STRING; 224325.AF_0723; -.
DR EnsemblBacteria; AAB90519; AAB90519; AF_0723.
DR GeneID; 24794321; -.
DR KEGG; afu:AF_0723; -.
DR eggNOG; arCOG04383; Archaea.
DR HOGENOM; CLU_820433_0_0_2; -.
DR OMA; NDHESDI; -.
DR OrthoDB; 57676at2157; -.
DR PhylomeDB; O29535; -.
DR UniPathway; UPA00148; UER00227.
DR EvolutionaryTrace; O29535; -.
DR Proteomes; UP000002199; 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 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..298
FT /note="Cobalt-precorrin-5B C(1)-methyltransferase"
FT /id="PRO_0000141690"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1SR8"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:1SR8"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:1SR8"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1SR8"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1SR8"
SQ SEQUENCE 298 AA; 33163 MW; ABED7A132D52E7AA CRC64;
MLIDPIELYR YPEKWIKDRD AEKKVRSGLY ILTEDGYLRR GITTGTTASA AAVAAIASLK
EKVEKVKVST PAGVDVEVEV EAEKGFARVR KFSGDHEFDV TNGIIFEAEV CETSGIFFGR
GVGVKAGEKA VSRSAKLQIL ENFIKASREF NFSGGVRISV PDGEEVAKKT GNEKVGIKGG
ISILGTTGFV EPWCKKLVET KLKIAMQYHR IAITTGRKAW LYARKKFPEY QPFVFGVHID
EALKHPGEKI IVGFPGLLKI WAGSRDRIEE RAREEGVRVV VIEDDMDSWV WDVQGTDH
