COBJ_SINSX
ID COBJ_SINSX Reviewed; 254 AA.
AC P21640;
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-3B C(17)-methyltransferase;
DE Short=Precorrin-3 methylase;
DE Short=Precorrin-3 methyltransferase;
DE EC=2.1.1.131;
GN Name=cobJ;
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=8226690; DOI=10.1128/jb.175.22.7430-7440.1993;
RA Debussche L., Thibaut D., Cameron B., Crouzet J., Blanche F.J.;
RT "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas
RT denitrificans.";
RL J. Bacteriol. 175:7430-7440(1993).
CC -!- FUNCTION: Methyltransferase that catalyzes the methylation of C-17 in
CC precorrin-3B to form precorrin-4.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=precorrin-3B + S-adenosyl-L-methionine = 3 H(+) + precorrin-4
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12761, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57769, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:77870; EC=2.1.1.131;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 3/10.
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; AAA25798.1; -; Genomic_DNA.
DR AlphaFoldDB; P21640; -.
DR SMR; P21640; -.
DR KEGG; ag:AAA25798; -.
DR BioCyc; MetaCyc:MON-85; -.
DR UniPathway; UPA00148; UER00214.
DR GO; GO:0030789; F:precorrin-3B C17-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11646; Precorrin_3B_C17_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; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR01466; cobJ_cbiH; 1.
PE 1: Evidence at protein level;
KW Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..254
FT /note="Precorrin-3B C(17)-methyltransferase"
FT /id="PRO_0000150402"
SQ SEQUENCE 254 AA; 27105 MW; A30B027F4AFBE23F CRC64;
MTGTLYVVGT GPGSAKQMTP ETAEAVAAAQ EFYGYFPYLD RLNLRPDQIR VASDNREELD
RAQVALTRAA AGVKVCMVSG GDPGVFAMAA AVCEAIDKGP AEWKSVELVI TPGVTAMLAV
AARIGAPLGH DFCAISLSDN LKPWEVITRR LRLAAEAGFV IALYNPISKA RPWQLGEAFE
LLRSVLPASV PVIFGRAAGR PDERIAVMPL GEADANRADM ATCVIIGSPE TRIVERDGQP
DLVYTPRFYA GASQ