QORH_SPIOL
ID QORH_SPIOL Reviewed; 329 AA.
AC Q8H0M1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Quinone-oxidoreductase homolog, chloroplastic;
DE EC=1.-.-.-;
DE AltName: Full=ceQORH;
GN Name=QOR;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-32; 39-51; 54-64; 92-112;
RP 157-177; 196-220 AND 270-280, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf;
RX PubMed=12368288; DOI=10.1074/jbc.m207477200;
RA Miras S., Salvi D., Ferro M., Grunwald D., Garin J., Joyard J., Rolland N.;
RT "Non-canonical transit peptide for import into the chloroplast.";
RL J. Biol. Chem. 277:47770-47778(2002).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12368288}.
CC -!- DOMAIN: Neither the N-terminal nor the C-terminal are essential for
CC chloroplastic localization of the protein. An internal region (59-Pro-
CC Ala-100) is essential but not sufficient for plastid localization.
CC -!- PTM: The transit peptide is not cleaved.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ511792; CAD54431.1; -; mRNA.
DR AlphaFoldDB; Q8H0M1; -.
DR SMR; Q8H0M1; -.
DR OrthoDB; 727365at2759; -.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Membrane; NAD; Oxidoreductase;
KW Plastid; Plastid inner membrane.
FT CHAIN 1..329
FT /note="Quinone-oxidoreductase homolog, chloroplastic"
FT /id="PRO_0000160916"
SQ SEQUENCE 329 AA; 34811 MW; 908A03516336890E CRC64;
MAAKLMHAIQ YSGYGGGTDA LKHVEVAVPD PKSDELLLKI EAATLNPIDW KIQKGVLRPL
LPRKFPTIPG TDVAGEVVQA GSAVNRFKTG DKVVAVLSHA TGGALAEYAV AKENLTVARP
PEVSAAEGAA LPVAALTAHQ ALTQFANIKL DGSGERKNIL ITAASGGVGH YAVQLAKLGN
THVTATCGAR NLDFVKGLGA DEVLDYKTPE GASLTSPSGK KYDYVVHGAS GIPWSTFEPN
LSEAGKVIDL TPGPTAMMTF AWKKLTFSKK QLVPLLLIPK IPNFEYVVNL VKEKKLKTVI
DSKHPLSKGE DAWSRIMGGH ATGKIIIEP