NU2C_PROM0
ID NU2C_PROM0 Reviewed; 506 AA.
AC A3PBF7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NAD(P)H dehydrogenase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1, subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=ndhB {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=P9301_04591;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_00445}.
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_00445};
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_00445};
CC -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC different subcomplexes with different compositions have been identified
CC which probably have different functions. {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; CP000576; ABO17082.1; -; Genomic_DNA.
DR RefSeq; WP_011862457.1; NC_009091.1.
DR AlphaFoldDB; A3PBF7; -.
DR SMR; A3PBF7; -.
DR STRING; 167546.P9301_04591; -.
DR EnsemblBacteria; ABO17082; ABO17082; P9301_04591.
DR KEGG; pmg:P9301_04591; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_2_3; -.
DR OMA; FYIRVIV; -.
DR Proteomes; UP000001430; 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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="NAD(P)H-quinone oxidoreductase subunit 2"
FT /id="PRO_1000026150"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 506 AA; 54016 MW; 75A2F8EAEE281809 CRC64;
MPNEIFTINL NAQAIIPEAF ILLGIVGTLL VDLAGEKTAS KWAPSICYLS IGSSLLSLTL
QWNNPVESAF LGSFNSDNLA IAFRAIIALS TLVSLLISWR YTEQSGSPIG EFAAIVLSAT
LGAMLLCGST DLISVFISLE TLSVASYLLS GYLKRDPRSS EAALKYLLVG SAAAAVYLYG
SSFLYGLSGS TNLTTIGLEI INKPSFITSL ALVFVLSTVA FKIAAVPFHQ WTPDVYEGSP
TPVVAFLSVG SKTAGFAFAI RILSTTFSSF DEEWKLLFTI LAILSMALGN VVALAQTSMK
RMLAYSSIGQ AGFVMIGIVS GTQDGLSAAV LYLAAYLFMN LGAFSCVILF SLRTGSDRIL
DYSGLYQKDP LITLGLSLCL LSLGGLPPML GFFGKIYLFF AGWANHQYLL VIVGLVTSVI
SIYYYISVIK MMVVKEPQEA SEIVKSYPEV NWGIAGLPPL RVALYTCVAV TALGGILSNP
LFKLANTAVS ETPFLQDVIA AANNIS
