ID   CBIL_METJA              Reviewed;         230 AA.
AC   Q58181;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Probable cobalt-precorrin-2 C(20)-methyltransferase;
DE            EC=2.1.1.151;
DE   AltName: Full=S-adenosyl-L-methionine--cobalt-precorrin-2 methyltransferase;
GN   Name=cbiL; OrderedLocusNames=MJ0771;
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).
CC   -!- FUNCTION: Methylates cobalt-precorrin-2 at the C-20 position to produce
CC       cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17997,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:60053, ChEBI:CHEBI:60060; EC=2.1.1.151;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 2/10.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; L77117; AAB98764.1; -; Genomic_DNA.
DR   PIR; C64396; C64396.
DR   AlphaFoldDB; Q58181; -.
DR   SMR; Q58181; -.
DR   STRING; 243232.MJ_0771; -.
DR   EnsemblBacteria; AAB98764; AAB98764; MJ_0771.
DR   KEGG; mja:MJ_0771; -.
DR   eggNOG; arCOG00648; Archaea.
DR   HOGENOM; CLU_076014_2_1_2; -.
DR   InParanoid; Q58181; -.
DR   OMA; MEYPVTT; -.
DR   PhylomeDB; Q58181; -.
DR   UniPathway; UPA00148; UER00224.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0043781; F:cobalt-factor II C20-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11645; Precorrin_2_C20_MT; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR012382; CobI/CbiL.
DR   InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036427; Precrrn-2_mtase; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01467; cobI_cbiL; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..230
FT                   /note="Probable cobalt-precorrin-2 C(20)-methyltransferase"
FT                   /id="PRO_0000150411"
SQ   SEQUENCE   230 AA;  26267 MW;  4FFD926E9B441FFB CRC64;
     MNKLVKKVYG VGVGVGDKKL LTLKALEVLK KVDKIFVPVS KKGKKSIAYE IIKDYVDGKN
     IEELLFPMIK DKERLKKYWE NALEKVLKED GEVAIITIGD PTLYSTFSYV WKLLKERGVE
     VEIVNGISSI FASAAALNIP LVEGDEKLCI LPQGKDLEKY IDEFDTIIIM KTKNLNEKLS
     VIKNRDDYII GLVKRATFED EKVVIGKLDE INFDEFNDYL SLAIIKRFKR