NU5C_MAIZE
ID NU5C_MAIZE Reviewed; 738 AA.
AC P46620;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 112.
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; Synonyms=ndh5;
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-709.
RC TISSUE=Leaf;
RA Clark L.G., Zhang W., Wendel J.F.;
RL Submitted (FEB-1995) 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; X86563; CAA60346.1; -; Genomic_DNA.
DR EMBL; U21985; AAA64703.1; -; Genomic_DNA.
DR PIR; S58612; S58612.
DR RefSeq; NP_043084.1; NC_001666.2.
DR AlphaFoldDB; P46620; -.
DR SMR; P46620; -.
DR STRING; 4577.GRMZM5G894515_P01; -.
DR PaxDb; P46620; -.
DR PRIDE; P46620; -.
DR GeneID; 845185; -.
DR KEGG; zma:845185; -.
DR MaizeGDB; 107782; -.
DR eggNOG; KOG4668; Eukaryota.
DR HOGENOM; CLU_007100_6_1_1; -.
DR OMA; QIFITVE; -.
DR OrthoDB; 526738at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR Genevisible; P46620; ZM.
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:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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 Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..738
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118191"
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 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 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 268
FT /note="Missing (in Ref. 2; AAA64703)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="W -> L (in Ref. 2; AAA64703)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="R -> G (in Ref. 2; AAA64703)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="K -> R (in Ref. 2; AAA64703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 82976 MW; F4E3EBD0DD3C91FA CRC64;
MEHTYQYAWV IPLLPLPVIM SMGFGLFLIP TATKNLRRIW AFPSILLLSI AMVFSLHLSI
QQINGSSIYQ YLWSWTINND FSLEFGYLVD PLTSIMLILI TTVGILVLIY SDDYMSHDEG
YLRFFVYISF FNTSMLGLVT SSNLIQIYFF WELVGMCSYL LIGFWFTRPI AASACQKAFV
TNRVGDFGLL LGILGFFWIT GSLEFRDLFK IANNWIPNNG INSLLTTLCA FLLFLGAVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLLARL LPLFISLPWI MSFISLIGTI
TLFLGATLAL AQRDIKRSLA YSTMSQLGYM MLALGIGSYQ AALFHLITHA YSKALLFLGS
GSVIHSMEPL VGYSPDKSQN MVLMGGLRKY VPITRTTFLC GTLSLCGIPP LACFWSKDEI
LSNSWLYSPF FGIIASFTAG LTAFYMFRIY LLTFDGYLRV HFQNYSSTKE GSLYSISLWG
KSISKGVNRD FVLSTMKSGV SFFSQNIPKI PANTRNKIGS FSTPFGAKNT FVYPHETGNT
MLFPLLILLL FTLFIGSIGI HFDNGVKDNR ILELTILSKW LTPSINLFQE NSNSSINSYE
FLTNAISSVS LAIFGLFIAY IFYGSAYSFF QNLNFQNSLV KKNPKKSFLD EVKKKIYSWS
YNRGYIDFFY TRVFILGIRK LAELTHFFDK GVIDGITNGV GLAGFCIGEE IKYVGGGRIS
SYLFFFLCYV SLFLFFIP
