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NADH-quinone oxidoreductase subunit H (EC 1.6.5.11) (NADH dehydrogenase I subunit H) (NDH-1 subunit H)

 H2FC75_9ASPA            Unreviewed;       363 AA.
H2FC75;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
27-SEP-2017, entry version 21.
RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
EC=1.6.5.11 {ECO:0000256|HAMAP-Rule:MF_01350};
AltName: Full=NADH dehydrogenase I subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
AltName: Full=NDH-1 subunit H {ECO:0000256|HAMAP-Rule:MF_01350};
Name=ndhA {ECO:0000313|EMBL:AEX96258.1};
Synonyms=nuoH {ECO:0000256|HAMAP-Rule:MF_01350};
Hosta ventricosa (blue plantain lily).
Plastid {ECO:0000313|EMBL:AEX96258.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX96258.1};
[1] {ECO:0000313|EMBL:AFA27797.1}
NUCLEOTIDE SEQUENCE.
Givnish T.J., Ames M., McNeal J.R., McKain M.J., Steele P.R.,
dePamphilis C.W., Graham S.W., Pires J.C., Stevenson D.W.,
Zomlefer W.B., Briggs B.G., Duvall M.R., Moore M.J., Heaney J.M.,
Soltis D.E., Soltis P.S., Thiele K., Leebens-Mack J.H.;
"Assembling the Tree of the Monocotyledons: Plastome Sequence
Phylogeny and Evolution of Poales.";
Ann. Mo. Bot. Gard. 97:584-616(2010).
[2] {ECO:0000313|EMBL:AEX96258.1}
NUCLEOTIDE SEQUENCE.
PubMed=22291168; DOI=10.3732/ajb.1100491;
Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
Pires J.C.;
"Quality and quantity of data recovered from massively parallel
sequencing: Examples in Asparagales and Poaceae.";
Am. J. Bot. 99:330-348(2012).
[3] {ECO:0000313|EMBL:APO12275.1}
NUCLEOTIDE SEQUENCE.
PubMed=27793858;
McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
Leebens-Mack J.;
"Timing of rapid diversification and convergent origins of active
pollination within Agavoideae (Asparagaceae).";
Am. J. Bot. 103:1717-1729(2016).
-!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
sulfur (Fe-S) centers, to quinones in the respiratory chain. The
immediate electron acceptor for the enzyme in this species is
believed to be ubiquinone. Couples the redox reaction to proton
translocation (for every two electrons transferred, four hydrogen
ions are translocated across the cytoplasmic membrane), and thus
conserves the redox energy in a proton gradient. This subunit may
bind ubiquinone. {ECO:0000256|HAMAP-Rule:MF_01350}.
-!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
NuoA, H, J, K, L, M, N constitute the membrane sector of the
complex. {ECO:0000256|HAMAP-Rule:MF_01350}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01350, ECO:0000256|RuleBase:RU000471}; Multi-pass membrane
protein {ECO:0000256|HAMAP-Rule:MF_01350,
ECO:0000256|RuleBase:RU000471}.
-!- SIMILARITY: Belongs to the complex I subunit 1 family.
{ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01350}.
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EMBL; JQ276436; AEX96258.1; -; Genomic_DNA.
EMBL; HQ180909; AFA27797.1; -; Genomic_DNA.
EMBL; KX931460; APO12275.1; -; Genomic_DNA.
RefSeq; YP_009335217.1; NC_032706.1.
GeneID; 30766991; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
HAMAP; MF_01350; NDH1_NuoH; 1.
InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
PANTHER; PTHR11432; PTHR11432; 1.
Pfam; PF00146; NADHdh; 1.
PROSITE; PS00667; COMPLEX1_ND1_1; 1.
PROSITE; PS00668; COMPLEX1_ND1_2; 1.
3: Inferred from homology;
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01350};
Chloroplast {ECO:0000313|EMBL:AEX96258.1};
Membrane {ECO:0000256|HAMAP-Rule:MF_01350};
NAD {ECO:0000256|HAMAP-Rule:MF_01350, ECO:0000256|RuleBase:RU000471};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01350,
ECO:0000256|RuleBase:RU000471}; Plastid {ECO:0000313|EMBL:AEX96258.1};
Quinone {ECO:0000256|HAMAP-Rule:MF_01350};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01350};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01350};
Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01350}.
TRANSMEM 26 50 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
TRANSMEM 95 116 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
TRANSMEM 122 147 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
TRANSMEM 254 277 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
TRANSMEM 297 322 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
TRANSMEM 343 361 Helical. {ECO:0000256|HAMAP-
Rule:MF_01350}.
NON_TER 363 363 {ECO:0000313|EMBL:AFA27797.1}.
SEQUENCE 363 AA; 40100 MW; 8A2BB4D1E67C5A80 CRC64;
MIIDTTEVQA INSFSRSESL KEVYGLIWIF VPIFTLILGI TIGVLVIVWL EREISAAIQQ
RIGPEYAGPL GILQALADGT KLLFKEDLLP SRGDIRLFSV GPSIAVISVL LSYLVIPFES
RLVLADLSIG VFLWISISSI APIGLLMSGY GSNNKYSFSG GLRAAAQSIS YEIPLTLCVL
SISLLSNSLS TVDIVEAQSK YGFWGWNLWR QPIGFVVFLI SSLAECERLP FDLPEAEEEL
VAGYQTEYSG IKYALFYLAS YLNLLVSSLF ITVLYLGGWN FSIPYISIPA LFGINKMAGV
FGMTIGIFIT LAKAYLFLFI PITARWTLPR MRMDQLLNLG WKFLLPISLG NLLLTTSSQL
VSL


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