NU5C_DIGGR
ID NU5C_DIGGR Reviewed; 699 AA.
AC Q32131;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 5;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5;
DE Flags: Fragment;
GN Name=ndhF;
OS Digitalis grandiflora (Yellow foxglove).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Digitalideae; Digitalis.
OX NCBI_TaxID=38791;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Olmstead R.G., Reeves P.A.;
RT "Evidence for the polyphyly of the Scrophulariaceae based on chloroplast
RT rbcL and ndhF sequences.";
RL Ann. Mo. Bot. Gard. 82:176-193(1995).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; L36399; AAA84203.1; -; Genomic_DNA.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF01010; Proton_antipo_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..>699
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118182"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 699
SQ SEQUENCE 699 AA; 79311 MW; 5685FBA561C63D01 CRC64;
WIIPFVPLPV PMLIGVGLLL FPIXTNKLRR MWAFPSILLL SIVMIFSTNL SIQQINSNSI
YQYVWSWTLD NDFSLELGCL IDPLTSIMSM LITIVGITVL IYSDNYMAHD QGYLRFFAYM
SFFSTSMLGL VTSSNLIQIY IFWELVGVCS YLLIGFWFTR PLAANACQKA FVTNRVGDFG
LLLGILGFYW ITGSFEFRDL FEIFNNLIVN NQVNYLFVTL CAALLFAGAV AKSAQFPLHV
WLPDAMEGPT PISALIHAAT MVAEGIFLVA RLLPLFIVIP YIMNFISLIG IITVLLGATL
ALAQKDIKRG LAYSTMSQLG YMMLALGMGS YRSALFHLIT HAYSKALLFL GSGSVIHSME
TIVGYSPEKS QNMVLMGGLR KYVPITKISF LLGTLSLCGI PPLACFWSKD EILNDSWLYS
PIFAIIAWAT AGLTAFYMFR IYLLTFEGHL NVYFQNYSGK KNTAFYSISI WGKGCSKRIN
KNFRLLRINN QSSSFFLKKT YRSDENLKKR NGGRPFINLI RFENKKARLY PYESDNTMLF
PLLILVLFTL FVGYLGISFN QEARDLDILS KWLAPSIDLL HQKSRDLTDW YEFLKDAIFS
VSIAYFGILL ASLLYKPIFA SFKNFDLINS FVKTGPKRSR WDKILTLLYN WSHNRAYIDV
FYTTSFTGSI RGLSQLTHFF DTQVIDGITN GVGVMSFFV