ID   COBG_SINSX              Reviewed;         459 AA.
AC   P21637;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Precorrin-3B synthase;
DE            EC=1.14.13.83;
GN   Name=cobG;
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 elimination of C-20 in precorrin-3A to form
CC       precorrin-3B.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + NADH + O2 + precorrin-3A = H2O + NAD(+) + precorrin-
CC         3B; Xref=Rhea:RHEA:17293, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58561, ChEBI:CHEBI:77870; EC=1.14.13.83;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 2/10.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {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; AAA25795.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21637; -.
DR   SMR; P21637; -.
DR   BioCyc; MetaCyc:MON-84; -.
DR   UniPathway; UPA00148; UER00213.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043818; F:precorrin-3B synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.413.10; -; 2.
DR   InterPro; IPR012798; Cbl_synth_CobG-like.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   SUPFAM; SSF56014; SSF56014; 2.
DR   TIGRFAMs; TIGR02435; CobG; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cobalamin biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding;
KW   NAD; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN           1..459
FT                   /note="Precorrin-3B synthase"
FT                   /id="PRO_0000199966"
FT   BINDING         338
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         344
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         377
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         381
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  46691 MW;  EC101F4C1FDC7209 CRC64;
     MTDLMTSCAL PLTGDAGTVA SMRRGACPSL AEPMQTGDGL LVRVRPTDDS LTLPKVIALA
     TAAERFGNGI IEITARGNLQ LRGLSAASVP RLAQAIGDAE IAIAEGLAIE VPPLAGIDPD
     EIADPRPIAT ELREALDVRQ VPLKLAPKLS VVIDSGGRFG LGAVVADIRL QAVSTVAGVA
     WVLSLGGTST KASSVGTLAG NAVVPALITI LEKLASLGTT MRGRDLDPSE IRALCRCETS
     SERPAAPRSA AIPGIHALGN ADTVLGLGLA FAQVEAAALA SYLHQVQALG ANAIRLAPGH
     AFFVLGLCPE TAAVAQSLAA SHGFRIAEQD PRNAIATCAG SKGCASAWME TKGMAERLVE
     TAPELLDGSL TVHLSGCAKG CARPKPSELT LVGAPSGYGL VVNGAANGLP SAYTDENGMG
     SALARLGRLV RQNKDAGESA QSCLTRLGAA RVSAAFEQG