CBIT_METJA
ID CBIT_METJA Reviewed; 183 AA.
AC Q57836;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00786};
DE EC=2.1.1.196 {ECO:0000255|HAMAP-Rule:MF_00786};
GN Name=cbiT {ECO:0000255|HAMAP-Rule:MF_00786}; OrderedLocusNames=MJ0391;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=23688113; DOI=10.1186/1472-6807-13-10;
RA Padmanabhan B., Yokoyama S., Bessho Y.;
RT "Crystal structure of putative CbiT from Methanocaldococcus jannaschii: an
RT intermediate enzyme activity in cobalamin (vitamin B12) biosynthesis.";
RL BMC Struct. Biol. 13:10-10(2013).
CC -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B
CC followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
CC {ECO:0000255|HAMAP-Rule:MF_00786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00786};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type
CC CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}.
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DR EMBL; L77117; AAB98376.1; -; Genomic_DNA.
DR PIR; G64348; G64348.
DR PDB; 2YXD; X-ray; 2.30 A; A/B=1-183.
DR PDBsum; 2YXD; -.
DR AlphaFoldDB; Q57836; -.
DR SMR; Q57836; -.
DR STRING; 243232.MJ_0391; -.
DR EnsemblBacteria; AAB98376; AAB98376; MJ_0391.
DR KEGG; mja:MJ_0391; -.
DR eggNOG; arCOG00977; Archaea.
DR HOGENOM; CLU_094143_0_0_2; -.
DR InParanoid; Q57836; -.
DR OMA; RCKFVYA; -.
DR PhylomeDB; Q57836; -.
DR UniPathway; UPA00148; UER00229.
DR EvolutionaryTrace; Q57836; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00786; CbiT; 1.
DR InterPro; IPR023475; CbiT.
DR InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02469; CbiT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..183
FT /note="Probable cobalt-precorrin-6B C(15)-methyltransferase
FT (decarboxylating)"
FT /id="PRO_0000134938"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 43..47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00786"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2YXD"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 150..164
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2YXD"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2YXD"
SQ SEQUENCE 183 AA; 20502 MW; CB47419BB8781340 CRC64;
MKYMIPDEEF IRREGVPITK EEIRAVSIGK LNLNKDDVVV DVGCGSGGMT VEIAKRCKFV
YAIDYLDGAI EVTKQNLAKF NIKNCQIIKG RAEDVLDKLE FNKAFIGGTK NIEKIIEILD
KKKINHIVAN TIVLENAAKI INEFESRGYN VDAVNVFISY AKKIPSGHMF LAKNPITIIK
AVR
