NU5C_POPAL
ID NU5C_POPAL Reviewed; 760 AA.
AC Q14FB0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
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;
GN Name=ndhF;
OS Populus alba (White poplar).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Okumura S., Yamashita A., Kanamoto H., Hattori M., Takase H., Tomizawa K.;
RT "Complete structure of the chloroplast genome of Populus alba.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008956; BAE97252.1; -; Genomic_DNA.
DR RefSeq; YP_665604.1; NC_008235.1.
DR AlphaFoldDB; Q14FB0; -.
DR SMR; Q14FB0; -.
DR GeneID; 4178232; -.
DR KEGG; palz:4178232; -.
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..760
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360968"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 760 AA; 86045 MW; 5F5EFF7C1D50EF6F CRC64;
MEHTYQYLWI ISFVTLPVPM LIGMGLLLFP VSTKKLHRIW AFPSVLLLSI VMVFSTDLFI
QQINSSSIYQ YVWSWTINND FSLEFGHLID PLTSILLILI TTVGILVLVY SDSYMSHDQG
YLRFFVYMSF FNTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPI VSNACQKAFV
TNRVGDFGLL LGILGLYWIT GSFEFQDLFE IFNNLIYNND NEVHFLFVTL CAFLLFSGAI
AKSAQFPLHV WLPDAMEGPT PISALIHAAT MVAAGIFLVA RLLPLFVVIP YIMKLIALIG
IITVLLGATL AFAQKDIKRG LAYSTMSQLG YTMLALGMGS YRAALFHLIT HAYSKALLFL
GSGSIIHSME GIVGYSPDKS QNMVLMGGLT KHVPITKIAF LLGTLSLCGI PPLACFWSKD
EILNDSWSYS PIFAIIAFST AGLTAFYMFR VYLLTFEGHL NIYFQNYSGK KNSAFYSISL
WGKQGSKILK KKMRLLPLLT INNKNNNERA SFFCFFWKKI YQTGGTVRKM TCPFITINHF
GTKRIFSYPQ ESDNTILFPM LVLVLFTLFI GAIGIPFNQF NKEEMNLDIL SKLLIPSLSL
LHQNQNESVD WYEFVTNSTF SVSIASFGIF IASSLYKPIY SSLQNLKFLN LVAKKGPKRI
LWDKIINVIY DWSYNRGYID VFYTISLTEG IRRLAELTSF FDRRVIDGIT NGVGFTSFFA
GEGIKYVGGG RISFYLLLYL FYVLIFLLIS SSIFSSFSSL
