NU2C_SYNJB
ID NU2C_SYNJB Reviewed; 527 AA.
AC Q2JLH4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=CYB_1471;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000240; ABD02437.1; -; Genomic_DNA.
DR RefSeq; WP_011433085.1; NC_007776.1.
DR AlphaFoldDB; Q2JLH4; -.
DR SMR; Q2JLH4; -.
DR STRING; 321332.CYB_1471; -.
DR KEGG; cyb:CYB_1471; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_3; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000001938; 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..527
FT /note="NAD(P)H-quinone oxidoreductase subunit 2"
FT /id="PRO_0000391236"
FT TRANSMEM 11..31
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 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 106..126
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 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 527 AA; 55672 MW; 13CE9F0681550E8E CRC64;
MDVFAPTGNL YAGAIWPEVV VTLTLLLVLV VDLVGGSAAR KSLPALSIFG LIGALVTLVL
QWQQPQLESF LGSFAADPVS ILFRGLVVGT AVLTVMMAER YIAQSGAPTG EFYVLLLTAT
LGGMFLSGAT DLILVFVSLE TLGIASYLMA GYTKRDPRSS EAALKYLLIG ASSTAIFLYG
MSLLYGLSGG QTKLEAIASS MGDAGLAGII ALVLCIGGIG FKLAAVPFHQ WTPDVYEGSP
TPVVAFLSVG SKAAGFALAV RFLATVFPAM TEEWRAVLSV LAILTMVLGN VVAIAQTRLK
RLLAYSSIGQ AGFVMIGLVV GTEAGYASLI FYLLVYLVMN LGAFLCITLF SLKTGTDEIN
EYSGLYQKDP FLTLCLSICL LSLGGLPPLA GFFGKLYLFW AGWQAGAYTL VLVGLVTSVI
SIYYYVRVVK TIVVKEPQEM SVSVQNYPET NWQAEGMPAL RVGMVLTLVA TIFAGILSNP
LFTLSIQAVE QSPFLGFPTA QAPIPESASL QVAVDGSLGS LTQPSQG
