NU5C2_PAUCH
ID NU5C2_PAUCH Reviewed; 618 AA.
AC B1X5V5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, organellar chromatophore 2;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 5 2;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 2;
GN Name=ndhF2; OrderedLocusNames=PCC_0915;
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore.
OC Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(2008).
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, organellar chromatophore thylakoid
CC membrane {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; CP000815; ACB43324.1; -; Genomic_DNA.
DR RefSeq; YP_002049534.1; NC_011087.1.
DR AlphaFoldDB; B1X5V5; -.
DR SMR; B1X5V5; -.
DR GeneID; 6481703; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR010217; NU5C2.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01960; ndhF3_CO2; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone;
KW Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..618
FT /note="NAD(P)H-quinone oxidoreductase subunit 5, organellar
FT chromatophore 2"
FT /id="PRO_0000360977"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 618 AA; 66676 MW; 7EA1FF38ECE5D8A8 CRC64;
MSLSTVLSLS TQFAWLIPIY GFAGMVVSLP WATGWIQRNA PRTPAYLNLI ISLVAFLHGS
LALQDVLQNG AHIIRFPWLN LSQADLQLNI SLDISPTNLA ALELITGLSF IAQLYALGYL
DKEWALARFF ALAGFFEGAM SGVVLSDSLF QSYFLLEMLT LSTYLLVGFW YAQPLVVTAA
RDAFLTKRVG DVMLLMGVVA LSAFAGGMEF EDLYTWADKN TLTPLATTLL GLALIAGPIG
KCAQFPMHLW LDEAMEGPNP ASILRNSVVV TCGAIVLMKL MPILHHSQIT IAVLLAIGTI
SALGGSLVSI AQVDIKRTLS YSTTAYLGLV FIAIALEQPA LALLTLFAHA IAKALLSMSI
GSVIAVSNCQ DITELGGLGS RMPATTSAYL IAGAGLTGLL PLGCFWCFGL GMDLIGRQAP
WFASIYLITN TLTALNLTRV FRQVFLGAPM PKTRRAAEVN WQMALPMVVL LVAVALTPWM
MARIDPLPGI GAFSAITGIT VATSGLVGLT IGAIVPLNKA WSRSLNQPVR WVQDLLAFDF
YTDRFYRLTI VNIVSGCSYI ASWFDTAIVN GFVNYVGRFS MDSAEGLRLS ISGRSQSYIL
TVVITIVFLL AALSWLVS
