ID   NQO2_PONAB              Reviewed;         231 AA.
AC   Q5RBB9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone];
DE            EC=1.10.5.1;
DE   AltName: Full=NRH dehydrogenase [quinone] 2;
DE   AltName: Full=NRH:quinone oxidoreductase 2;
DE   AltName: Full=Quinone reductase 2;
DE            Short=QR2;
GN   Name=NQO2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC       connection with conjugation reactions of hydroquinones involved in
CC       detoxification pathways as well as in biosynthetic processes such as
CC       the vitamin K-dependent gamma-carboxylation of glutamate residues in
CC       prothrombin synthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone +
CC         H(+) = a quinol + beta-nicotinamide D-riboside; Xref=Rhea:RHEA:12364,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:55458, ChEBI:CHEBI:132124; EC=1.10.5.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than
CC       NAD(P)H as an electron donor.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC       {ECO:0000305}.
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DR   EMBL; CR858732; CAH90941.1; -; mRNA.
DR   RefSeq; NP_001127353.1; NM_001133881.1.
DR   AlphaFoldDB; Q5RBB9; -.
DR   SMR; Q5RBB9; -.
DR   STRING; 9601.ENSPPYP00000023806; -.
DR   GeneID; 100174417; -.
DR   KEGG; pon:100174417; -.
DR   CTD; 4835; -.
DR   eggNOG; ENOG502QWY5; Eukaryota.
DR   InParanoid; Q5RBB9; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..231
FT                   /note="Ribosyldihydronicotinamide dehydrogenase [quinone]"
FT                   /id="PRO_0000071628"
FT   BINDING         12
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         18..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..151
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16083"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16083"
SQ   SEQUENCE   231 AA;  26144 MW;  2CAD61FD15A415DA CRC64;
     MAGKKVLIVY AHQEPRSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATKKDITGAL
     SNPEVFHYGV ETHEAYKQRS LASDITDEQK KVQEADLVIF QFPLYWFSVP AILKGWMDRV
     LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDFRYFLW PLQHGTLHFC
     GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWYFR Q