ID   COBK_RHOCB              Reviewed;         251 AA.
AC   O68098; D5AV05;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Precorrin-6A reductase;
DE            EC=1.3.1.54;
DE   AltName: Full=Precorrin-6X reductase;
GN   Name=cobK; OrderedLocusNames=RCAP_rcc02043;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA   Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT   "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT   SB1003.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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}.
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DR   EMBL; AF010496; AAC16188.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85787.1; -; Genomic_DNA.
DR   PIR; T03535; T03535.
DR   RefSeq; WP_013067766.1; NC_014034.1.
DR   PDB; 4X7G; X-ray; 1.22 A; A=1-251.
DR   PDB; 5C4N; X-ray; 1.63 A; D=1-251.
DR   PDB; 5C4R; X-ray; 3.17 A; A=1-251.
DR   PDBsum; 4X7G; -.
DR   PDBsum; 5C4N; -.
DR   PDBsum; 5C4R; -.
DR   AlphaFoldDB; O68098; -.
DR   SMR; O68098; -.
DR   STRING; 272942.RCAP_rcc02043; -.
DR   EnsemblBacteria; ADE85787; ADE85787; RCAP_rcc02043.
DR   GeneID; 31490905; -.
DR   KEGG; rcp:RCAP_rcc02043; -.
DR   eggNOG; COG2099; Bacteria.
DR   HOGENOM; CLU_068627_1_0_5; -.
DR   OMA; THPYAAQ; -.
DR   OrthoDB; 1726104at2; -.
DR   UniPathway; UPA00148; UER00217.
DR   Proteomes; UP000002361; Chromosome.
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   3D-structure; Cobalamin biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..251
FT                   /note="Precorrin-6A reductase"
FT                   /id="PRO_0000135921"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           52..63
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           77..90
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           116..122
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           139..144
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          148..156
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          165..171
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           205..212
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:4X7G"
FT   HELIX           234..243
FT                   /evidence="ECO:0007829|PDB:4X7G"
SQ   SEQUENCE   251 AA;  26048 MW;  877B825031DB202F CRC64;
     MTRLLVLGGT TEASRLAKTL ADQGFEAVFS YAGRTGAPVA QPLPTRIGGF GGVAGLVDYL
     TREGVSHVID ATHPFAAQMS ANAVAACAQT GVALCAFERA PWTAQAGDRW THVPDLAAAV
     AALPQAPARV FLAIGKQHLR DFSAAPQHHY LLRLVDPPEG PLPLPDARAV IARGPFTVQG
     DTELLRSETI THVVAKNAGG AGAEAKLIAA RSLGLPVILI DRPAVPARDI CATLEGVMGW
     LADHGATPRG V