NU3C_THEVB
ID NU3C_THEVB Reviewed; 132 AA.
AC Q8DJ02;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 3;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 3;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 3;
DE AltName: Full=NDH-1 subunit 3;
DE Short=NDH-C;
GN Name=ndhC; OrderedLocusNames=tlr1429;
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-8 AND 53-73, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15910282; DOI=10.1042/bj20050390;
RA Zhang P., Battchikova N., Paakkarinen V., Katoh H., Iwai M., Ikeuchi M.,
RA Pakrasi H.B., Ogawa T., Aro E.-M.;
RT "Isolation, subunit composition and interaction of the NDH-1 complexes from
RT Thermosynechococcus elongatus BP-1.";
RL Biochem. J. 390:513-520(2005).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
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DR EMBL; BA000039; BAC08981.1; -; Genomic_DNA.
DR RefSeq; NP_682219.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; C=1-132.
DR PDB; 6KHI; EM; 3.00 A; C=1-132.
DR PDB; 6KHJ; EM; 3.00 A; C=1-132.
DR PDB; 6L7O; EM; 3.20 A; C=1-132.
DR PDB; 6L7P; EM; 3.60 A; C=1-132.
DR PDB; 6NBQ; EM; 3.10 A; C=1-132.
DR PDB; 6NBX; EM; 3.50 A; C=1-132.
DR PDB; 6NBY; EM; 3.10 A; C=1-132.
DR PDB; 6TJV; EM; 3.20 A; C=1-132.
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; Q8DJ02; -.
DR SMR; Q8DJ02; -.
DR IntAct; Q8DJ02; 1.
DR STRING; 197221.22295153; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08981; BAC08981; BAC08981.
DR KEGG; tel:tlr1429; -.
DR PATRIC; fig|197221.4.peg.1500; -.
DR eggNOG; COG0838; Bacteria.
DR OMA; RFPVKYY; -.
DR OrthoDB; 1748431at2; -.
DR Proteomes; UP000000440; 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:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.1610; -; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; NAD; NADP;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15910282"
FT CHAIN 2..132
FT /note="NAD(P)H-quinone oxidoreductase subunit 3"
FT /id="PRO_0000362786"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 19..42
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6L7O"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 103..125
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:6NBQ"
SQ SEQUENCE 132 AA; 15003 MW; DC2E8C8DDF6155B0 CRC64;
MVAIPRLRDT ATVFVLSGYE YFLGFLIICS LVPVLALAAS ALLRPKSGRM IRLTTYESGM
EPIGGAWIQF NVRYYMFALV FVIFDVETVF LYPWAVAFHQ LGLLAFIEAL IFIAILVVAL
VYAWRKRALE WS
