NU2C_PROMT
ID NU2C_PROMT Reviewed; 520 AA.
AC Q46GY3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=PMN2A_1767;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
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; CP000095; AAZ59255.1; -; Genomic_DNA.
DR RefSeq; WP_011294400.1; NC_007335.2.
DR AlphaFoldDB; Q46GY3; -.
DR SMR; Q46GY3; -.
DR STRING; 59920.PMN2A_1767; -.
DR EnsemblBacteria; AAZ59255; AAZ59255; PMN2A_1767.
DR KEGG; pmn:PMN2A_1767; -.
DR HOGENOM; CLU_007100_1_2_3; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR PhylomeDB; Q46GY3; -.
DR Proteomes; UP000002535; 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..520
FT /note="NAD(P)H-quinone oxidoreductase subunit 2"
FT /id="PRO_0000225357"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 520 AA; 55018 MW; D90BDDB8644DCD71 CRC64;
MGELLSFQIF INEPVELLNL SLNAKAVLPE AAVLMAMLGT LLVDLAGEKI SARWSPPICY
AGLGSALILL AMQWDGEIQE SFLGAFIADN LAIAFRGVIV LSTLISLLIS WRYADQNGSP
IGEFAAILLA ATLGAMLLCG STDLVSVFVS LETLSVASYL LSGYLKRDSR SSEAALKYLL
VGSAAAAVFL YGASLLYGIS GSTNLKEIGT TLLSAPTPLS ALALVFVLST VAFKIAAVPF
HQWTPDVYEG SPTPVVAFLS VGSKAAGFAL AIRILVGCFS AFDTQWKLLF TVLAVLSMSL
GNVVALAQKS MKRMLAYSSI GQAGFVMIGL VCGTEDGFAA MVLYMAAYLF MNLGAFACII
LFSIRTGSDQ ISDYAGLYQK DPLITLGLSL CLLSLGGIPP MLGFFGKIYL FFAGWADGQY
LLVTVGLVTS VISIYYYISV IKMMVVTEPK EASDVVKAYP SIEWSIPGMS SLKVALIFCV
LVTAIGGIIS NPLFNFADSA VNGTPLLREA ITLASKSSIG
