ID D3EQS8_ATETH Unreviewed; 394 AA.
AC D3EQS8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE Short=NDH-H {ECO:0000256|HAMAP-Rule:MF_01358};
GN Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358};
GN OrderedLocusNames=UCYN_11590 {ECO:0000313|EMBL:ADB95828.1};
OS Atelocyanobacterium thalassa (isolate ALOHA).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Atelocyanobacterium;
OC Candidatus Atelocyanobacterium thalassa.
OX NCBI_TaxID=1453429 {ECO:0000313|Proteomes:UP000001405};
RN [1] {ECO:0000313|EMBL:ADB95828.1, ECO:0000313|Proteomes:UP000001405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALOHA {ECO:0000313|Proteomes:UP000001405};
RX PubMed=20173737; DOI=10.1038/nature08786;
RA Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F.,
RA Affourtit J.P., Zehr J.P.;
RT "Metabolic streamlining in an open-ocean nitrogen-fixing cyanobacterium.";
RL Nature 464:90-94(2010).
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01358}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01358}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC ECO:0000256|RuleBase:RU003685}.
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DR EMBL; CP001842; ADB95828.1; -; Genomic_DNA.
DR RefSeq; WP_012954515.1; NC_013771.1.
DR AlphaFoldDB; D3EQS8; -.
DR STRING; 1453429.UCYN_11590; -.
DR KEGG; cyu:UCYN_11590; -.
DR PATRIC; fig|713887.8.peg.1085; -.
DR HOGENOM; CLU_015134_1_2_3; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000001405; 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; Cytochrome-c3 Hydrogenase, chain B; 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 NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01358};
KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000001405};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01358};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01358};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 124..394
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 394 AA; 45489 MW; 92C6FC82A430911F CRC64;
MSKIETRTEP MVINMGPHHP SMHGVLRLIV TLDGEDVVDC EPVIGYLHRG MEKIAENRTN
IMYVPYVSRW DYAAGMFNEA ITVNAPEKLA NIKVPKRAQY IRVIMLELNR IANHLLWLGP
FLADVGATTP FFYIFREREM IYDLWEAASG MRLINNNYFR IGGVAVDLPY GWIDKCEDFC
NHFKTKVDEY EKLITNNPIF RRRIEGIGKI AREDAINWGL SGPMLRGSGV KWDLRKVDHY
ECYDDFDWDI QWETEGDCLA RYFVRIKEMR ESVKILSQAL KGIPGGPYEN LEAKRMIEGK
KSQWDDFDYQ YIAKKVAPTF KIPSGEHYVR LESGKGELGI FIIGNNDVFP WRWKIRAPDF
NNLQILPHLL KGVKVADIMA ILGSIDVIMG SVDR
//
