ID   COBF_SINSX              Reviewed;         261 AA.
AC   P21636;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Precorrin-6A synthase [deacetylating];
DE            EC=2.1.1.152;
GN   Name=cobF;
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).
CC   -!- FUNCTION: Catalyzes the methylation of C-1 in precorrin-5 and the
CC       subsequent extrusion of acetic acid from the resulting intermediate to
CC       form cobalt-precorrin-6A.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + precorrin-5 + S-adenosyl-L-methionine = acetate + 2 H(+)
CC         + precorrin-6A + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18261,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77871,
CC         ChEBI:CHEBI:77872; EC=2.1.1.152;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 5/10.
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; AAA25794.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21636; -.
DR   SMR; P21636; -.
DR   BioCyc; MetaCyc:MON-87; -.
DR   UniPathway; UPA00148; UER00216.
DR   GO; GO:0043819; F:precorrin-6A synthase (deacetylating) 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; cd11643; Precorrin-6A-synthase; 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; IPR012797; CobF.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036525; CobF; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR02434; CobF; 1.
PE   4: Predicted;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..261
FT                   /note="Precorrin-6A synthase [deacetylating]"
FT                   /id="PRO_0000150400"
SQ   SEQUENCE   261 AA;  28945 MW;  7798AB0CCDF4A008 CRC64;
     MAEAGMRKIL IIGIGSGNPE HMTVQAINAL NCADVLFIPT KGAKKTELAE VRRDICARYV
     TRKDSRTVEF AVPVRRTEGV SYDGSVDDWH AQIAGIYEAL LSKELGEEGT GAFLVWGDPM
     LYDSTIRIVE RVKARGEVAF AYDVIPGITS LQALCASHRI PLNLVGKPVE ITTGRRLHES
     FPEKSQTSVV MLDGEQAFQR VEDPEAEIYW GAYLGTRDEI VISGRVAEVK DRILETRAAA
     RAKMGWIMDI YLLRKGADFD E