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Database: UniProt
Entry: Q1ACE5
LinkDB: Q1ACE5
Original site: Q1ACE5 
ID   NDHI_CHAVU              Reviewed;         159 AA.
AC   Q1ACE5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   16-JAN-2019, entry version 63.
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   Chara vulgaris (Common stonewort).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales;
OC   Characeae; Chara.
OX   NCBI_TaxID=55564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16611644; DOI=10.1093/molbev/msk018;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The chloroplast genome sequence of Chara vulgaris sheds new light
RT   into the closest green algal relatives of land plants.";
RL   Mol. Biol. Evol. 23:1324-1338(2006).
CC   -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       photosynthetic chain and possibly in a chloroplast respiratory
CC       chain. The immediate electron acceptor for the enzyme in this
CC       species is believed to be plastoquinone. Couples the redox
CC       reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01351}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol
CC         + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000255|HAMAP-Rule:MF_01351};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol
CC         + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62192; 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
CC       which are encoded in the nucleus. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; DQ229107; ABA61901.1; -; Genomic_DNA.
DR   RefSeq; YP_635802.1; NC_008097.1.
DR   ProteinModelPortal; Q1ACE5; -.
DR   SMR; Q1ACE5; -.
DR   GeneID; 4100271; -.
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   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; PTHR10849; PTHR10849; 1.
DR   PANTHER; PTHR10849:SF23; PTHR10849:SF23; 1.
DR   Pfam; PF13237; Fer4_10; 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;
KW   NADP; Plastid; Plastoquinone; Quinone; Repeat; Thylakoid; Translocase.
FT   CHAIN         1    159       NAD(P)H-quinone oxidoreductase subunit I,
FT                                chloroplastic.
FT                                /FTId=PRO_0000250766.
FT   DOMAIN       55     84       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN       95    124       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        64     64       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        67     67       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        70     70       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        74     74       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       104    104       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       110    110       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       114    114       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   159 AA;  18628 MW;  F322FF8BE0306BB4 CRC64;
     MFNFINSLKN YSQESFRAAR YIGQGFIVTL NHINRSAITV QYPYEKLITS ERFRGRIHFE
     FDKCIVCEVC VRVCPINLPV VDWNFQQDIR KKKLKNYSID FGVCIFCGNC VEYCPTNCLS
     MTEEYELSVY DRHELNYDQI ALGRLPFNSF QDALVTKAS
//
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