QOR_KLUMA
ID QOR_KLUMA Reviewed; 380 AA.
AC Q8NJJ9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=NADPH quinone oxidoreductase {ECO:0000303|PubMed:14536026};
DE EC=1.6.5.2 {ECO:0000269|PubMed:14536026};
DE Flags: Precursor;
GN Name=QOR {ECO:0000303|PubMed:14536026};
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14536026; DOI=10.5483/bmbrep.2003.36.5.442;
RA Kim W.H., Chung J.H., Back J.H., Choi J., Cha J.H., Koh H.Y., Han Y.S.;
RT "Molecular cloning and characterization of an NADPH quinone oxidoreductase
RT from Kluyveromyces marxianus.";
RL J. Biochem. Mol. Biol. 36:442-449(2003).
CC -!- FUNCTION: NADPH quinone oxidoreductase that efficiently reduces 1,4-
CC benzoquinone, whereas no activities are found for menadiones and
CC methoxyquinones. {ECO:0000269|PubMed:14536026}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:14536026};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:14536026};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for 1,4-benzoquinone {ECO:0000269|PubMed:14536026};
CC KM=298.2 mM for 2,3-dichloro-5,6-dicyano-1,4-benzoquinone
CC {ECO:0000269|PubMed:14536026};
CC KM=728.6 mM for phenyl-1,4-benzoquinone
CC {ECO:0000269|PubMed:14536026};
CC KM=647.5 mM for hydroquinone {ECO:0000269|PubMed:14536026};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14536026}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AY040868; AAK77939.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJJ9; -.
DR SMR; Q8NJJ9; -.
DR BRENDA; 1.6.5.10; 1120.
DR SABIO-RK; Q8NJJ9; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; NADP; Oxidoreductase; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..380
FT /note="NADPH quinone oxidoreductase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431099"
SQ SEQUENCE 380 AA; 41782 MW; BC91015792093ECC CRC64;
MSSFLSKRFI STTQRAMSQL PKAKSLIYSS HDQDVSKILK VHTYQPKGSA ESSILLKTLA
FPINPSDINQ LEGVYPSKPE KVLDYSTEKP SAIAGNKGLF EVVSLPSGVK NLKAGDRVIP
LQANFGTWST YRTCESENDL IKIEGVDLYT AATIAVNGCT AYQMVNDYIE WDPSGNDWLV
QNAGTSSVSK IVTQIAKDKG IKTLSVVRDR DNFDEVAENL EKKYGATKVI SESQNGEREF
GNEVLPKILG PNAQVKLALN SVGGKSCTNI ARKLSPNGLM LTYGGMSKQP VTLPTGLFIF
NSIRSHGFWV TANSKRDPEN KRKTVDAVVK LYRDGKIISP KEDIRTLEWD VNNLSDEGVL
DLVNRGIATK GAKNMVVLKW
