ID   NDHH_SYNJB              Reviewed;         392 AA.
AC   Q2JN25;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NAD(P)H dehydrogenase subunit H;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01358};
DE            Short=NDH-H {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=CYB_0872;
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_01358}.
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_01358};
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_01358};
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_01358}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; CP000240; ABD01852.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2JN25; -.
DR   SMR; Q2JN25; -.
DR   STRING; 321332.CYB_0872; -.
DR   PRIDE; Q2JN25; -.
DR   KEGG; cyb:CYB_0872; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_3; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..392
FT                   /note="NAD(P)H-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000371936"
SQ   SEQUENCE   392 AA;  44970 MW;  86ABA4055F35C64D CRC64;
     MIETRTDRML LNFGPHHPSM HGVLRLLVTL DGENIVDCEP VIGYLHRGME KIAENRTVVQ
     YLPYVSRWDY GAGMFNEAIT VNAVEKLAGI SVPRRASYLR VIMLELTRIT NHLLWFGPFL
     ADLGAQTPFL YAMREREWIL DLFEAVTGMR LINNNYFRVG GVAVDLPYGW TEKCLDFCEY
     FLPKVDEYER LVTDNPIFRR RLEGVGAISK QDAINWGLSG PMLRACGVNW DLRKVDHYEC
     YDDFDWEVAV YPEGDCLARY RVRMKEMRES CKIVQQAVKA LPGGPFENLE AKRMLEGPKS
     EWNKGDYQFI SKKPSANFKI PKGEAYVRVE SAKGELGIYI VGDDNVCPWR WKIRPPGFVN
     LQVLPQLIRG MKVADMIAIL GSIDIIMGEV DR