NU4C1_SYNP2
ID NU4C1_SYNP2 Reviewed; 534 AA.
AC B1XHP2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 92.
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};
GN OrderedLocusNames=SYNPCC7002_A1973;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000951; ACA99960.1; -; Genomic_DNA.
DR RefSeq; WP_012307583.1; NC_010475.1.
DR AlphaFoldDB; B1XHP2; -.
DR SMR; B1XHP2; -.
DR STRING; 32049.SYNPCC7002_A1973; -.
DR EnsemblBacteria; ACA99960; ACA99960; SYNPCC7002_A1973.
DR KEGG; syp:SYNPCC7002_A1973; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_0_3; -.
DR OMA; RIACSSV; -.
DR Proteomes; UP000001688; 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; IPR000260; NADH4_N.
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; 2.
DR Pfam; PF01059; Oxidored_q5_N; 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..534
FT /note="NAD(P)H-quinone oxidoreductase chain 4 1"
FT /id="PRO_0000343250"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 376..396
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"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 534 AA; 57894 MW; 716A82E305785643 CRC64;
MDSLQIPWLT TAIAFPLLAA LVIPLIPDKE GKTIRWYTLG VALTDFALLV TAFWQNYDLG
RTEFQLTENF AWIPQLGLNW SLGVDGLSMP LIILATLITT LATLAAWNVT KKPKLFAGLI
LVMLSAQIGV FAVQDLLLFF IMWELELVPV YLLISIWGGK KRLYAATKFI LYTALGSVFI
LASTLALAFY GGDVTFDMQA LGLKDYPLAL ELLAYAGFLI GFGVKLPIFP LHTWLPDAHS
EASAPVSMIL AGVLLKMGGY GLIRLNMEML PDAHIRFAPL LIVLGIVNIV YGALTAFGQT
NLKRRLASSS ISHMGFVLVG IASFTDLGMN GAVLQMLSHG FIAAALFFLS GVTYERTHTL
MMDEMSGIAR LMPKTFAMFT AAAMASLALP GMSGFVSELT VFLGLSNSDA YSYGFKAIAI
FLTAVGVILT PIYLLSMLRE VFYGKGSQAP LSLAAGEDAK PREIFVAVCL LAPIIAIGLY
PKLATTTYDL KTVEVASKVR AALPLYAEQL PQNGDRQAQM GLSSQMPALI APRF
