NU5C_SYNP2
ID NU5C_SYNP2 Reviewed; 664 AA.
AC P31971; B1XII7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 5;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase I, chain 5;
DE AltName: Full=NDH-1, chain 5;
GN Name=ndhF; OrderedLocusNames=SYNPCC7002_A0854;
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 [GENOMIC DNA].
RX PubMed=8501038; DOI=10.1128/jb.175.11.3343-3352.1993;
RA Schluchter W.M., Zhao J., Bryant D.A.;
RT "Isolation and characterization of the ndhF gene of Synechococcus sp.
RT strain PCC 7002 and initial characterization of an interposon mutant.";
RL J. Bacteriol. 175:3343-3352(1993).
RN [2]
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.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=1554697; DOI=10.1021/bi00127a009;
RA Schluchter W.M., Bryant D.A.;
RT "Molecular characterization of ferredoxin-NADP+ oxidoreductase in
RT cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp.
RT PCC 7002 and studies on the gene product.";
RL Biochemistry 31:3092-3102(1992).
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 (By similarity). {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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; M99378; AAA27311.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA98858.1; -; Genomic_DNA.
DR EMBL; M86234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_012306482.1; NC_010475.1.
DR AlphaFoldDB; P31971; -.
DR SMR; P31971; -.
DR STRING; 32049.SYNPCC7002_A0854; -.
DR EnsemblBacteria; ACA98858; ACA98858; SYNPCC7002_A0854.
DR KEGG; syp:SYNPCC7002_A0854; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_3; -.
DR OMA; LIGFWQH; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 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 Cell membrane; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="NAD(P)H-quinone oxidoreductase chain 5"
FT /id="PRO_0000118209"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
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 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 40
FT /note="N -> Y (in Ref. 1; AAA27311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 72878 MW; F8AE5DA8A1F8F26B CRC64;
MEPLYQYAWL IPVLPLLGAM VIGIGLISLN KFTNKLRQLN AVFVLSLIGT SMALSFGLLW
SQIQGHEAFT YTLEWAAAGD FHLQMGYTVD HLSALMSVIV TTVALLVMIY TDGYMAHDPG
YVRFYAYLSI FSSSMLGLVF SPNLVQVYIF WELVGMCSYL LIGFWYDRKA AADACQKAFV
TNRVGDFGLL LGMLGLYWAT GSFEFDLMGD RLMDLVSTGQ ISSLLAIVFA VLVFLGPVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGVFLVARM YPVFEPIPEA MNVIAWTGAT
TAFLGATIAL TQNDIKKGLA YSTMSQLGYM VMAMGIGGYT AGLFHLMTHA YFKAMLFLGS
GSVIHGMEEV VGHNAVLAQD MRLMGGLRKY MPITATTFLI GTLAICGIPP FAGFWSKDEI
LGLAFEANPV LWFIGWATAG MTAFYMFRMY FLTFEGEFRG TDQQLQEKLL TAAGQAPEEG
HHGSKPHESP LTMTFPLMAL AVPSVLIGLL GVPWGNRFEA FVFSPNEAAE AAEHGFELTE
FLIMGGNSVG IALIGITIAS LMYLQQRIDP ARLAEKFPVL YQLSLNKWYF DDIYNNVFVM
GTRRLARQIL EVDYRVVDGA VNLTGIATLL SGEGLKYIEN GRVQFYALIV FGAVLGFVIF
FSVA
