GenomeNet

Database: UniProt
Entry: A4QJH0
LinkDB: A4QJH0
Original site: A4QJH0 
ID   NDHI_AETCO              Reviewed;         167 AA.
AC   A4QJH0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   16-JAN-2019, entry version 60.
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   Aethionema cordifolium (Lebanon stonecress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
OC   Aethionemeae; Aethionema.
OX   NCBI_TaxID=434059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Aethionema coridifolium chloroplast DNA.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; AP009366; BAF49825.1; -; Genomic_DNA.
DR   RefSeq; YP_001123000.1; NC_009265.1.
DR   ProteinModelPortal; A4QJH0; -.
DR   SMR; A4QJH0; -.
DR   PRIDE; A4QJH0; -.
DR   GeneID; 4968590; -.
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; PF13187; Fer4_9; 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    167       NAD(P)H-quinone oxidoreductase subunit I,
FT                                chloroplastic.
FT                                /FTId=PRO_0000298565.
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   167 AA;  19454 MW;  8E0B88050EE2D275 CRC64;
     MLPMITGFMN YGQQTLRAAR YIGQGFMITL SHTNRLPVTI QYPYEKLITS ERFRGRIHFE
     FDKCIACEVC VRVCPIDLPV VDWKLETPIR KKRLLNYSID FGICIFCGNC VEYCPTNCLS
     MTEEYEFSTY DRHELNYNQI ALGRLPISVI DDYTIRTILN SPQIKNG
//
DBGET integrated database retrieval system