ID   COBK_SINSX              Reviewed;         261 AA.
AC   P21920;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Precorrin-6A reductase;
DE            EC=1.3.1.54;
DE   AltName: Full=Precorrin-6X reductase;
GN   Name=cobK;
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   PROTEIN SEQUENCE OF 2-7; 60-69; 112-122 AND 143-148, SEQUENCE REVISION, AND
RP   CHARACTERIZATION.
RX   PubMed=1732193; DOI=10.1128/jb.174.3.1036-1042.1992;
RA   Blanche F., Thibaut D., Famechon A., Debussche L., Cameron B., Crouzet J.;
RT   "Precorrin-6x reductase from Pseudomonas denitrificans: purification and
RT   characterization of the enzyme and identification of the structural gene.";
RL   J. Bacteriol. 174:1036-1042(1992).
CC   -!- FUNCTION: Catalyzes the reduction of the macrocycle of precorrin-6X
CC       into precorrin-6Y.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A;
CC         Xref=Rhea:RHEA:23408, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58532, ChEBI:CHEBI:77872; EC=1.3.1.54;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 6/10.
CC   -!- SIMILARITY: Belongs to the precorrin-6x reductase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00356}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25799.1; Type=Miscellaneous discrepancy; Note=Originally thought to be encoded on the other DNA strand, the correct open reading frame was subsequently identified.; Evidence={ECO:0000305|PubMed:1732193};
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DR   EMBL; M59301; AAA25799.1; ALT_SEQ; Genomic_DNA.
DR   PIR; F36145; F36145.
DR   AlphaFoldDB; P21920; -.
DR   SMR; P21920; -.
DR   BioCyc; MetaCyc:MON-113; -.
DR   UniPathway; UPA00148; UER00217.
DR   GO; GO:0016994; F:precorrin-6A reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003723; Precorrin-6x_reduct.
DR   PANTHER; PTHR36925; PTHR36925; 1.
DR   Pfam; PF02571; CbiJ; 1.
DR   TIGRFAMs; TIGR00715; precor6x_red; 1.
DR   PROSITE; PS51014; COBK_CBIJ; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1732193"
FT   CHAIN           2..261
FT                   /note="Precorrin-6A reductase"
FT                   /id="PRO_0000135920"
SQ   SEQUENCE   261 AA;  28096 MW;  B0AE2E902D35F02C CRC64;
     MAGSLFDTSA MEKPRILILG GTTEARELAR RLAEDVRYDT AISLAGRTAD PRPQPVKTRI
     GGFGGADGLA HFVHDENIAL LVDATHPFAA RISHNAADAA QRTGVALIAL RRPEWVPLPG
     DRWTAVDSVV EAVSALGDRR RRVFLAIGRQ EAFHFEVAPQ HSYVIRSVDP VTPPLNLPDQ
     EAILATGPFA EADEAALLRS RQIDVIVAKN SGGSATYGKI AAARRLGIEV IMVERRKPAD
     VPTVGSCDEA LNRIAHWLAP A