NU5C_GOSBA
ID NU5C_GOSBA Reviewed; 745 AA.
AC A0ZZ82;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 47.
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 Gossypium barbadense (Sea-island cotton) (Egyptian cotton).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17159292; DOI=10.1266/ggs.81.311;
RA Ibrahim R.I.H., Azuma J., Sakamoto M.;
RT "Complete nucleotide sequence of the cotton (Gossypium barbadense L.)
RT chloroplast genome with a comparative analysis of sequences among 9 dicot
RT plants.";
RL Genes Genet. Syst. 81:311-321(2006).
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; AP009123; BAF41294.1; -; Genomic_DNA.
DR RefSeq; YP_913233.1; NC_008641.1.
DR AlphaFoldDB; A0ZZ82; -.
DR SMR; A0ZZ82; -.
DR GeneID; 4575199; -.
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..745
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360936"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 745 AA; 84612 MW; C12B3AD1FC31897B CRC64;
MEHADQYSWI IPFVPLPIPI LIGMGLLLFP TATKRLLLFP TATKNLRRMW AFPNILLLSI
VMIFSLDLSI QQINGSSIYQ YVWSWTINND FSFEFGYFID SLTSIMSILI TTVGIFVLIY
SDNYMSHDEG YLRFFAYMSL FNTSMLGLVT SCNLIQIYIF WELVGMCSYL LIGFWFTRPA
AANACQKAFV TNRIGDFGLL LGILGFYWIT GSFEFQDLFE IFNNLIYNNE VHFLFVTLCA
SLLFAGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL FPLFIVIPYI
MNLISLIGII TVLLGATLAL AQNDIKRGLA YSTMSQLGYM MLALGMGSYR AALFHLITHA
YSKALLFLAS GSIIHSMEAI VGYSPEKSQN MVFMGGLRKH VPVTQIAFLV GTLSLCGIPP
LACFWSKDEI LSDSWLYSPI FAIIAWSTAG LTAFYMFRIY LLTFEGHLNV HFQKYSGKKS
SSFYSIKLWG KEEQKIINRN FRLFPLLTLT MNNNEQPYTI GGKKEARITI TNFGYKKAFS
YPHESDNTML FPMLILLLFT LFVGAIAIPF NQEGMHLDIL SKLLTPSINL LHQNSNDFED
SYQFFKNATF SVSIACFGIF TAFLLYKPFY SSVQNLNLLN SFVKRGPKRI LLDKMIYLIY
DWSYNRGYID MFYSISLTKG IRGLAELTHF FDRRVIDGIT NGVGITSFFV GESVKYLGGS
RISFYLLLYL VYVFIFLVIS YFILF
