ID   COBL_SINSX              Reviewed;         413 AA.
AC   P21921;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Precorrin-6Y C(5,15)-methyltransferase [decarboxylating];
DE            Short=Precorrin-6 methyltransferase;
DE            Short=Precorrin-6Y methylase;
DE            EC=2.1.1.132;
GN   Name=cobL;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=2211521; DOI=10.1128/jb.172.10.5980-5990.1990;
RA   Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F.,
RA   Thibaut D., Debussche L.;
RT   "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans
RT   fragment carrying eight genes involved in transformation of precorrin-2 to
RT   cobyrinic acid.";
RL   J. Bacteriol. 172:5980-5990(1990).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1732195; DOI=10.1128/jb.174.3.1050-1052.1992;
RA   Blanche F., Famechon A., Thibaut D., Debussche L., Cameron B., Crouzet J.;
RT   "Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the biosynthetic
RT   sequence from precorrin-6y to precorrin-8x is catalyzed by the cobL gene
RT   product.";
RL   J. Bacteriol. 174:1050-1052(1992).
CC   -!- FUNCTION: Catalyzes the methylation of both C-5 and C-15 in precorrin-
CC       6Y to form precorrin-8X.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) +
CC         precorrin-8X + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17477,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58532, ChEBI:CHEBI:58581, ChEBI:CHEBI:59789;
CC         EC=2.1.1.132;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 7/10.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M59301; AAA25800.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21921; -.
DR   SMR; P21921; -.
DR   KEGG; ag:AAA25800; -.
DR   BioCyc; MetaCyc:MON-114; -.
DR   UniPathway; UPA00148; UER00218.
DR   GO; GO:0046025; F:precorrin-6Y C5,15-methyltransferase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd11644; Precorrin-6Y-MT; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; IPR012818; CbiE.
DR   InterPro; IPR006365; Cbl_synth_CobL.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036428; CobL; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR02467; CbiE; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..413
FT                   /note="Precorrin-6Y C(5,15)-methyltransferase
FT                   [decarboxylating]"
FT                   /id="PRO_0000150408"
SQ   SEQUENCE   413 AA;  42938 MW;  C78E174A79F94249 CRC64;
     MADVSNSEPA IVSPWLTVIG IGEDGVAGLG DEAKRLIAEA PVVYGGHRHL ELAASLITGE
     AHNWLSPLER SVVEIVARRG SPVVVLASGD PFFFGVGVTL ARRIASAEIR TLPAPSSISL
     AASRLGWALQ DATLVSVHGR PLDLVRPHLH PGARVLTLTS DGAGPRDLAE LLVSSGFGQS
     RLTVLEALGG AGERVTTQIA ARFMLGLVHP LNVCAIEVAA DEGARILPLA AGRDDALFEH
     DGQITKREVR ALTLSALAPR KGELLWDIGG GSGSIGIEWM LADPTMQAIT IEVEPERAAR
     IGRNATMFGV PGLTVVEGEA PAALAGLPQP DAIFIGGGGS EDGVMEAAIE ALKSGGRLVA
     NAVTTDMEAV LLDHHARLGG SLIRIDIARA GPIGGMTGWK PAMPVTQWSW TKG