NU5C_CUCSA
ID NU5C_CUCSA Reviewed; 748 AA.
AC Q2QD43; Q4VZM1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 Cucumis sativus (Cucumber).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekmibaekdadagi;
RX PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA Choi D.-W., Liu J.R., Cho K.Y.;
RT "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT Baekmibaekdadagi) chloroplast genome.";
RL Plant Cell Rep. 25:334-340(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Borszczagowski;
RX PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT genome: its composition and comparative analysis.";
RL Cell. Mol. Biol. Lett. 12:584-594(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chipper, and cv. Gy14;
RX PubMed=17546086; DOI=10.1139/g07-003;
RA Chung S.-M., Gordon V.S., Staub J.E.;
RT "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT differences between chilling-tolerant and -susceptible cucumber lines.";
RL Genome 50:215-225(2007).
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; DQ119058; AAZ94696.1; -; Genomic_DNA.
DR EMBL; AJ970307; CAJ00806.1; -; Genomic_DNA.
DR EMBL; DQ865975; ABI97461.1; -; Genomic_DNA.
DR EMBL; DQ865976; ABI98792.1; -; Genomic_DNA.
DR RefSeq; YP_247647.1; NC_007144.1.
DR AlphaFoldDB; Q2QD43; -.
DR SMR; Q2QD43; -.
DR GeneID; 3429258; -.
DR KEGG; csv:3429258; -.
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..748
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360928"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
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 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 154
FT /note="V -> G (in strain: cv. Borszczagowski)"
FT VARIANT 170
FT /note="T -> S (in strain: cv. Borszczagowski)"
FT VARIANT 175
FT /note="C -> G (in strain: cv. Borszczagowski)"
FT VARIANT 201
FT /note="G -> A (in strain: cv. Borszczagowski)"
FT VARIANT 513
FT /note="T -> I (in strain: cv. Borszczagowski)"
FT VARIANT 748
FT /note="F -> C (in strain: cv. Borszczagowski)"
SQ SEQUENCE 748 AA; 85207 MW; 2D0F298D51C06C68 CRC64;
MEYTYQYSWI IPFISLPIPI LIGVGLLLFP TATKNLRRLW SFPSILLLSI VMIFAVYLSI
DQINTSYIYQ YVWSWTINND FSLELGYFID PLTCIMAILI TTVGIMVLIY SDNYMSHDQG
YLRFFAYMSL FNTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPT AANACQKAFV
TNRVGDFGLL LGILGLYWTT GSFEFRDLFQ IFNNLIDNNE VNFLFLTLCA VLLFAGAVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIAIPYI MNLIALIGII
TVLFGATLAL AQKDIKRSLA YSTMSQLGYM MLALGMGSYQ AALFHLITHA YSKALLFLGS
GSIIHSMESV VGYSPDKSQN MVLMGGLTKH VPITKNAFLL GTLSLCGVPP LACFWSKDEI
LNDSWLYSPI FAIIACSTAG LTAFYMFRIY LLTFDGHLNL YCKNYSGKTN NSLYSISLWG
KEGSKIIKKN FPFFSLLTMN NKERSSFWMK KTTYPFNSNV TKKMRPFVSS PHFSTKNTFY
YPYESENTML FPMFVLSLFT LFVGVIGSPF TQFNQEAIDL NILDKWLTPS INLLHESSKD
SENWYEFVKN ATFSVTIAFF GIFIASFFYK PTYSSLQNLN FRNSFVKSFT KNFFFEKIIN
IIYNWSYNRG YIDTFYRISL IGGIRILAEL TYFFDRRIID GITNAVGILN FFVAESIKYV
GGGRISSYIL LYLVYLVIFI LVIYFVFF
