NU3C_SYNY3
ID NU3C_SYNY3 Reviewed; 120 AA.
AC P19045;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 124.
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=slr1279;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499764; DOI=10.1007/bf00332231;
RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.;
RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid DNA
RT and of the cyanobacterium Synechocystis sp. PCC6803.";
RL Mol. Gen. Genet. 216:60-69(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-6, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15102833; DOI=10.1074/jbc.m401107200;
RA Prommeenate P., Lennon A.M., Markert C., Hippler M., Nixon P.J.;
RT "Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:
RT identification of two new ndh gene products with nuclear-encoded homologues
RT in the chloroplast Ndh complex.";
RL J. Biol. Chem. 279:28165-28173(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15548534; DOI=10.1074/jbc.m410914200;
RA Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes
RT of Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 280:2587-2595(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; X17439; CAA35484.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18283.1; -; Genomic_DNA.
DR PIR; S04435; S04435.
DR AlphaFoldDB; P19045; -.
DR SMR; P19045; -.
DR IntAct; P19045; 3.
DR STRING; 1148.1653369; -.
DR PaxDb; P19045; -.
DR EnsemblBacteria; BAA18283; BAA18283; BAA18283.
DR KEGG; syn:slr1279; -.
DR eggNOG; COG0838; Bacteria.
DR InParanoid; P19045; -.
DR OMA; RFPVKYY; -.
DR PhylomeDB; P19045; -.
DR Proteomes; UP000001425; 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 Direct protein sequencing; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..120
FT /note="NAD(P)H-quinone oxidoreductase subunit 3"
FT /id="PRO_0000117859"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 120 AA; 13662 MW; 39343E8AFEAD8184 CRC64;
MFVLTGYEYF LGFLFICSLV PVLALTASKL LRPRDGGPER QTTYESGMEP IGGAWIQFNI
RYYMFALVFV VFDVETVFLY PWAVAFNQLG LLAFVEALIF IAILVVALVY AWRKGALEWS
