NU4C1_NOSS1
ID NU4C1_NOSS1 Reviewed; 538 AA.
AC Q8YZV7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NAD(P)H dehydrogenase I, chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NDH-1, chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
GN Name=ndhD1 {ECO:0000255|HAMAP-Rule:MF_00491}; OrderedLocusNames=alr0348;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_00491}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00491}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00491}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC {ECO:0000255|HAMAP-Rule:MF_00491}.
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DR EMBL; BA000019; BAB72306.1; -; Genomic_DNA.
DR PIR; AC1850; AC1850.
DR AlphaFoldDB; Q8YZV7; -.
DR SMR; Q8YZV7; -.
DR STRING; 103690.17129693; -.
DR EnsemblBacteria; BAB72306; BAB72306; BAB72306.
DR KEGG; ana:alr0348; -.
DR eggNOG; COG1008; Bacteria.
DR OMA; RIACSSV; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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 HAMAP; MF_00491; NDH1_NuoM; 1.
DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="NAD(P)H-quinone oxidoreductase chain 4 1"
FT /id="PRO_0000343229"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 538 AA; 58563 MW; 7B5AD67229495530 CRC64;
MMNLIEFPWL TAIIALPLVA ALAIPIIPDK EGKTVRWYGL GVAFADFALM IAAFWHYYDF
QSSSYQFVEK YAWVPQIGLN WSVAVDGLSM PLLLLTGLIN TLAIFAAWKV TNKPRLFYGL
MLVMYSAQLG VFVAQDLLLF FLMWEIELVP VYLLISIWGG PKRRYAATKF ILYTAAASIF
ILVAGFALAF SGDTVTFDIA ALGMKEYPKA IELLAYAGFL IAFGVKLPIF PLHTWLPDAH
GEASAPGSMI LAGVLLKMGG YALIRFNMEM LPDAHVYFAP VLAILGVVNI VYGACCAFAQ
TNLKRRLAYS SIAHMGFVLI GLASYTEIGV SGAVLQMVSH GLVAASLFFL TGVTYERTHT
LLMDKMGGIG KIMPKTFALY TAGAMASLAL PGMSGFVGEL MVFIGIATSD VYSSSFKVVV
VLLSAVGVIL TPIYLLSMLR QVFYGKQSDE LHLDAFVPDV KPRELFITAS LLLPIIGIGL
YPKLITQTYD AKTVEIAAHA RQVLPVVAGQ QPSSLYSQIF TAPTLANAQV ESLVNISK
