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Database: UniProt
Entry: A4GYX0
LinkDB: A4GYX0
Original site: A4GYX0 
ID   NDHI_POPTR              Reviewed;         176 AA.
AC   A4GYX0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   16-JAN-2019, entry version 75.
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};
GN   OrderedLocusNames=Poptr_cp083;
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera
OS   subsp. trichocarpa).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae;
OC   Populus.
OX   NCBI_TaxID=3694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually;
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D.,
RA   Boerjan W., Brun A., Brunner A., Busov V., Campbell M., Carlson J.,
RA   Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M.,
RA   Couturier J., Covert S., Cronk Q., Cunningham R., Davis J.,
RA   Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B.,
RA   Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K.,
RA   Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA   Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D.,
RA   Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M.,
RA   Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C.,
RA   Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S.,
RA   Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C.,
RA   Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G.,
RA   Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K.,
RA   Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H.,
RA   Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E.,
RA   Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T.,
RA   Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(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; EF489041; ABO36765.1; -; Genomic_DNA.
DR   RefSeq; YP_001109561.1; NC_009143.1.
DR   ProteinModelPortal; A4GYX0; -.
DR   PRIDE; A4GYX0; -.
DR   GeneID; 4929744; -.
DR   KEGG; pop:4929744; -.
DR   InParanoid; A4GYX0; -.
DR   KO; K05580; -.
DR   Proteomes; UP000006729; Chloroplast.
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; Complete proteome; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Repeat; Thylakoid; Translocase.
FT   CHAIN         1    176       NAD(P)H-quinone oxidoreductase subunit I,
FT                                chloroplastic.
FT                                /FTId=PRO_0000298586.
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   176 AA;  20528 MW;  20C2A0935C20236D CRC64;
     MFPMVTGFMN YGQQTVRAAR YIGQSFMTTL SHVNRLPVTI QYPYEKLITS ERFRGRIHFE
     FDKCIACEVC VRVCPIDLPV VDWELETNIR KKRLLNYSID FGICIFCGNC VEYCPTNCLS
     MTEEYELSTY NRHELNYNQI ALGRLPMSVI DDYTIRTILN SPQSLIKMVK PPLIKD
//
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