ID   NDBB_SYNY3              Reviewed;         404 AA.
AC   P73735;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Demethylphylloquinone reductase NdbB {ECO:0000303|PubMed:26023160};
DE            EC=1.6.5.12 {ECO:0000269|PubMed:26023160};
GN   Name=ndbB {ECO:0000303|PubMed:26023160}; OrderedLocusNames=slr1743;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000312|Proteomes:UP000001425};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26023160; DOI=10.1105/tpc.15.00103;
RA   Fatihi A., Latimer S., Schmollinger S., Block A., Dussault P.H.,
RA   Vermaas W.F., Merchant S.S., Basset G.J.;
RT   "A dedicated type II NADPH dehydrogenase performs the penultimate step in
RT   the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis.";
RL   Plant Cell 27:1730-1741(2015).
CC   -!- FUNCTION: Bifunctional oxidoreductase probably ables to act both on
CC       prenyl naphthoquinones and on prenyl benzoquinones (PubMed:26023160).
CC       Catalyzes the penultimate step in the biosynthesis of vitamin K1
CC       (PubMed:26023160). {ECO:0000269|PubMed:26023160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=demethylphylloquinone + H(+) + NADPH = demethylphylloquinol +
CC         NADP(+); Xref=Rhea:RHEA:47744, ChEBI:CHEBI:15378, ChEBI:CHEBI:31087,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87844; EC=1.6.5.12;
CC         Evidence={ECO:0000269|PubMed:26023160};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000305|PubMed:26023160};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by dicumarol.
CC       {ECO:0000269|PubMed:26023160}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.4 uM for menadione {ECO:0000269|PubMed:26023160};
CC         Note=kcat is 3.2 sec(-1) for menadione.
CC         {ECO:0000269|PubMed:26023160};
CC   -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC       {ECO:0000269|PubMed:26023160}.
CC   -!- DISRUPTION PHENOTYPE: Increased photosensitivity to high light.
CC       {ECO:0000269|PubMed:26023160}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17783.1; -; Genomic_DNA.
DR   PIR; S74822; S74822.
DR   AlphaFoldDB; P73735; -.
DR   SMR; P73735; -.
DR   IntAct; P73735; 2.
DR   STRING; 1148.1652865; -.
DR   PaxDb; P73735; -.
DR   EnsemblBacteria; BAA17783; BAA17783; BAA17783.
DR   KEGG; syn:slr1743; -.
DR   eggNOG; COG1252; Bacteria.
DR   OMA; ISDHHIR; -.
DR   PhylomeDB; P73735; -.
DR   SABIO-RK; P73735; -.
DR   UniPathway; UPA00995; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR   GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..404
FT                   /note="Demethylphylloquinone reductase NdbB"
FT                   /id="PRO_0000435625"
FT   BINDING         7..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..195
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  44489 MW;  AEFD093A05470CE3 CRC64;
     MTDARPRICI LGGGFGGLYT ALRLGQLSWE GHTPPEIVLV DQRDRFLFAP FLYELVTEEM
     QTWEIAPPFV ELLAESGVIF RQAEVTAIDF DHQKVLLNDQ DKGTESLAFD QLVIALGGQT
     PLPNLPGLKD YGLGFRTLED AYKLKQKLKS LEQADAEKIR IAIVGGGYSG VELAAKLGDR
     LGERGRIRII ERGKEILAMS PEFNRQQAQA SLSAKGIWVD TETTVTAITA TDVTLQFREQ
     EDVIPVDLVL WTVGTTVSPL IRNLALPHND QGQLRTNAQL QVEGKTNIFA LGDGAEGRDA
     SGQLIPTTAQ GAFQQTDYCA WNIWANLTGR PLLPCRYQPL GEMLALGTDG AVLSGLGIKL
     SGPAALLARR LVYLYRFPTW QHQLTVGLNW LTRPLGDWLK NEPS