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NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 1.6.5.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I)

 M9PIH2_EQUHY            Unreviewed;       182 AA.
M9PIH2;
26-JUN-2013, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01351};
EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01351};
AltName: Full=NAD(P)H dehydrogenase subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
Short=NDH subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
AltName: Full=NADH-plastoquinone oxidoreductase subunit I {ECO:0000256|HAMAP-Rule:MF_01351};
Name=ndhI {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000313|EMBL:AGC26679.1};
Equisetum hyemale (Dutch rush) (Scouring-rush horsetail).
Plastid; Chloroplast {ECO:0000313|EMBL:AGC26679.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Polypodiopsida; Equisetidae; Equisetales; Equisetaceae; Equisetum.
NCBI_TaxID=3262 {ECO:0000313|EMBL:AGC26679.1};
[1] {ECO:0000313|EMBL:AGC26679.1}
NUCLEOTIDE SEQUENCE.
PubMed=23311954; DOI=10.1186/1471-2148-13-8;
Grewe F., Guo W., Gubbels E.A., Hansen A.K., Mower J.P.;
"Complete plastid genomes from Ophioglossum californicum, Psilotum
nudum, and Equisetum hyemale reveal an ancestral land plant genome
structure and resolve the position of Equisetales among
monilophytes.";
BMC Evol. Biol. 13:8-8(2013).
-!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
FMN and iron-sulfur (Fe-S) centers, to quinones in the
photosynthetic chain and possibly in a chloroplast respiratory
chain. The immediate electron acceptor for the enzyme in this
species is believed to be plastoquinone. Couples the redox
reaction to proton translocation, and thus conserves the redox
energy in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911844}.
-!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911826}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_01351};
Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
Rule:MF_01351};
-!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of
which are encoded in the nucleus. {ECO:0000256|HAMAP-
Rule:MF_01351, ECO:0000256|SAAS:SAAS00911847}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|SAAS:SAAS00911824};
Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911824}.
-!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
{ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|SAAS:SAAS00911864}.
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EMBL; KC117177; AGC26679.1; -; Genomic_DNA.
RefSeq; YP_007374766.1; NC_020146.1.
GeneID; 14469342; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
HAMAP; MF_01351; NDH1_NuoI; 1.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR017900; 4Fe4S_Fe_S_CS.
InterPro; IPR004497; NADH_plast_OxRdtase_su_I.
InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
PANTHER; PTHR10849:SF23; PTHR10849:SF23; 1.
Pfam; PF13237; Fer4_10; 1.
TIGRFAMs; TIGR00403; ndhI; 1.
TIGRFAMs; TIGR01971; NuoI; 1.
PROSITE; PS00198; 4FE4S_FER_1; 1.
PROSITE; PS51379; 4FE4S_FER_2; 2.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00919365};
Chloroplast {ECO:0000256|SAAS:SAAS00911858,
ECO:0000313|EMBL:AGC26679.1};
Iron {ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|SAAS:SAAS00919365};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00919365};
Membrane {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911830};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00919365};
NAD {ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|SAAS:SAAS00919361};
NADP {ECO:0000256|HAMAP-Rule:MF_01351, ECO:0000256|SAAS:SAAS00911821};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00919366};
Plastid {ECO:0000256|SAAS:SAAS00911858, ECO:0000313|EMBL:AGC26679.1};
Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911862};
Quinone {ECO:0000256|HAMAP-Rule:MF_01351};
Repeat {ECO:0000256|SAAS:SAAS00919358};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_01351,
ECO:0000256|SAAS:SAAS00911841}.
DOMAIN 55 84 4Fe-4S ferredoxin-type.
{ECO:0000259|PROSITE:PS51379}.
DOMAIN 95 124 4Fe-4S ferredoxin-type.
{ECO:0000259|PROSITE:PS51379}.
METAL 64 64 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 67 67 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 70 70 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 74 74 Iron-sulfur 2 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 104 104 Iron-sulfur 2 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 107 107 Iron-sulfur 2 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 110 110 Iron-sulfur 2 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
METAL 114 114 Iron-sulfur 1 (4Fe-4S).
{ECO:0000256|HAMAP-Rule:MF_01351}.
SEQUENCE 182 AA; 21157 MW; 793207C5BD94CD53 CRC64;
MFSLLNGLRN YSEQAIQAAK YIGQGFSVTT DHMNRSPMTI QYPYEKLIPS ERFRGRIHFE
FDKCIACEVC VRVCPINLPV VDWDLKKDLR KKQLKNYSID FGICIFCGNC VEYCPTNCLS
MTEEYELSTY DRHDLNYDQI ALGRLPTPVV LDPMIQPIWN LNYLPKGLME GHSNSRTITH
FE


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