NU5C1_PAUCH
ID NU5C1_PAUCH Reviewed; 666 AA.
AC B1X491;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, organellar chromatophore 1;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 5 1;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 1;
GN Name=ndhF1; OrderedLocusNames=PCC_0319;
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; ACB42760.1; -; Genomic_DNA.
DR RefSeq; YP_002048970.1; NC_011087.1.
DR AlphaFoldDB; B1X491; -.
DR SMR; B1X491; -.
DR GeneID; 6481769; -.
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; 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 Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone;
KW Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..666
FT /note="NAD(P)H-quinone oxidoreductase subunit 5, organellar
FT chromatophore 1"
FT /id="PRO_0000360976"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
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 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 666 AA; 72959 MW; A510E4B9067C204C CRC64;
MLRRAVELVW LIPILPFIGA FLVGFGLISF NKKVNQLRKP AALLLISSVG ISAVLSFMVL
ADQIGGAPCS EVLFSWASAG TFNLEMGYRV DPIGATMLAL VSTVAILVMV YSDGYMSHDK
SYVRFFTYLG LFTSSMLALI LSPNLLEIYV FWELVGMCSY LLIGFWYERE DAANAAQKAF
VVNRVGDFGF LLGILGLFWA TNSFDFQIVA TKMAASISDG SIPHWAAIAL CLLLFMGPMA
KSAQFPLHVW LPDAMEGPTP ISALIHAATM VAAGVFLVAR LEPLYSQVPD VQIIVAVIGT
ITCFLGASIA LIQMDLKKGL AYSTISQLGY MMLAMGCGAP VAGMFHLITH AFFKAMLFLG
SGSVIHAMEE VVGHDPTLAQ DMRLMGGLRK TMPITGITFF IGCVAISGIP PLAGFWSKDE
ILSKAFDSYP LLWGVGLFTA GLTAFYMFRL YFLTFEGEFR GNNIALREKL LIAAGKSFDP
IETKEIQSTH ESGWQMTLPL VILSVPSVLI GFLGSPWNNR FGMLLYPEEA LEAAKTFSWG
EFLPLAIASV MISTCGIVIA TIAYAYHWID LGQSVASRLK IINNFLVNKW YLDKINEYIF
VNGSRGLAKK ILNLDETVLD KAVVETGLTT LDAGKWLSYF ETGRPQFYAL IIFGGVISLI
VIFNRL
