ID H9FQ79_MACMU Unreviewed; 329 AA.
AC H9FQ79;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Quinone oxidoreductase {ECO:0000256|ARBA:ARBA00039192};
DE EC=1.6.5.5 {ECO:0000256|ARBA:ARBA00038919};
DE AltName: Full=NADPH:quinone reductase {ECO:0000256|ARBA:ARBA00043088};
DE AltName: Full=Zeta-crystallin {ECO:0000256|ARBA:ARBA00042763};
GN Name=CRYZ {ECO:0000313|EMBL:AFE76788.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE76788.1};
RN [1] {ECO:0000313|EMBL:AFE76788.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE76788.1}, and Thymus
RC {ECO:0000313|EMBL:AFH31183.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone +
CC NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC EC=1.6.5.5; Evidence={ECO:0000256|ARBA:ARBA00036756};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR EMBL; JU333033; AFE76788.1; -; mRNA.
DR EMBL; JU474379; AFH31183.1; -; mRNA.
DR AlphaFoldDB; H9FQ79; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08253; zeta_crystallin; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 2: Evidence at transcript level;
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 17..327
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 35290 MW; 9670A2889B338C20 CRC64;
MATRQKLMRA VRVFEFGGPE VLKLQSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS
KKPLLPYTPG SDVAGLIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK
LDFKQGAAIG IPYFTACRAL IHSARVKAGE SVLVHGASGG VGLAACQIAR AYGLKVLGTA
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDV IIEMLANVNL SKDLSLLSHG
GRVIVVGNRG TIEINPRDTM AKESSIIGVT FFSSTKEEFQ QYAAALQAGM EIGWLKPVIG
SQYPLEKVAE AHKDIIHGSG ATGKMILLL
//
