NDHH_THEVB
ID NDHH_THEVB Reviewed; 394 AA.
AC Q8DJD9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=tlr1288;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08840.1; -; Genomic_DNA.
DR RefSeq; NP_682078.1; NC_004113.1.
DR RefSeq; WP_011057128.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; H=1-394.
DR PDB; 6KHI; EM; 3.00 A; H=1-394.
DR PDB; 6KHJ; EM; 3.00 A; H=1-394.
DR PDB; 6L7O; EM; 3.20 A; H=1-394.
DR PDB; 6L7P; EM; 3.60 A; H=1-394.
DR PDB; 6NBQ; EM; 3.10 A; H=1-394.
DR PDB; 6NBX; EM; 3.50 A; H=1-394.
DR PDB; 6NBY; EM; 3.10 A; H=1-394.
DR PDB; 6TJV; EM; 3.20 A; H=1-394.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DJD9; -.
DR SMR; Q8DJD9; -.
DR IntAct; Q8DJD9; 17.
DR STRING; 197221.22295012; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08840; BAC08840; BAC08840.
DR KEGG; tel:tlr1288; -.
DR PATRIC; fig|197221.4.peg.1355; -.
DR eggNOG; COG0649; Bacteria.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..394
FT /note="NAD(P)H-quinone oxidoreductase subunit H"
FT /id="PRO_0000357945"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6NBQ"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6NBY"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6KHJ"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 96..125
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 225..229
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 234..239
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6L7O"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6L7O"
FT HELIX 258..282
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6HUM"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:6KHJ"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6NBY"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 358..362
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6KHJ"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 394 AA; 45216 MW; 8E27898D7A82A965 CRC64;
MPKIETRTEP MVINMGPHHP SMHGVLRLMV TLDGEDVIDC EPVIGYLHRG MEKIAENRTN
IMFIPYVSRW DYAAGMFNEA VTVNAPEKLA GIPVPKRASY IRVIMLELNR IANHLLWLGP
FLADVGAQTP FFYIFREREY IYDLFEAATG MRFINNNYFR IGGVAADLTY GWVTKCRDFC
DYFLPKVDEY ERLITNNPIF VRRLQGVGKI SREEAINWGL SGPMLRASGV KWDLRKVDHY
ECYDDFDWDV PVATEGDCLA RYIVRIQEMR ESVKIIRQAL DGLPGGPYEN LEAKRMLEGA
KSEWNGFDYQ YIGKKLSPTF KIPKGEHYVR VESGKGELGI YLIGDDNVFP WRWKIRPPDF
NNLQVLPQLL KGMKVADIVA ILGSIDVIMG SVDR
