ID NDHI_LOXSI Reviewed; 166 AA. AC Q8HVQ0; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 22-FEB-2023, entry version 90. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01351}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NAD(P)H dehydrogenase subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE Short=NDH subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; GN Name=ndhI {ECO:0000255|HAMAP-Rule:MF_01351}; OS Loxothysanus sinuatus. OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; OC Heliantheae alliance; Bahieae; Loxothysanus. OX NCBI_TaxID=176551; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Panero J.L., Baldwin B.G., Schilling E.E., Clevinger J.A.; RT "Chloroplast DNA phylogeny of tribe Heliantheae (Asteraceae)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain CC and possibly in a chloroplast respiratory chain. The immediate electron CC acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, and CC thus conserves the redox energy in a proton gradient. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01351}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01351}. 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; AF383813; AAN61754.1; -; Genomic_DNA. DR AlphaFoldDB; Q8HVQ0; -. DR SMR; Q8HVQ0; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.70.3270; -; 1. DR HAMAP; MF_01351; NDH1_NuoI; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004497; NADH_plast_OxRdtase_su_I. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR PANTHER; PTHR47275; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT I, CHLOROPLASTIC; 1. DR PANTHER; PTHR47275:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT I, CHLOROPLASTIC; 1. DR Pfam; PF13187; Fer4_9; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR TIGRFAMs; TIGR00403; ndhI; 1. DR TIGRFAMs; TIGR01971; NuoI; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP; KW Plastid; Plastoquinone; Quinone; Repeat; Thylakoid; Translocase. FT CHAIN 1..166 FT /note="NAD(P)H-quinone oxidoreductase subunit I, FT chloroplastic" FT /id="PRO_0000250811" FT DOMAIN 55..84 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT DOMAIN 95..124 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 64 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 70 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 74 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 104 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 107 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 110 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 114 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" SQ SEQUENCE 166 AA; 19509 MW; 51D18659EA31BED7 CRC64; MFPMVTEFMN YGQQTVRAAR YIGQGFMITL SHANRLPVTI QYPYEKLITS ERFRGRIHFE FDKCIACEVC VRVCPIDLPV VDWKLETDIR KKRLLNYSID FGICIFCGNC VEYCPTNCLS MTEEYELSTY DRHELNYNQI ALGRLPMSII DDYTIRTIFN LPEIKT //