NU1C_SYNY3
ID NU1C_SYNY3 Reviewed; 372 AA.
AC P26522;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase I subunit 1;
DE AltName: Full=NDH-1 subunit 1;
DE AltName: Full=NDH-A;
GN Name=ndhA; OrderedLocusNames=sll0519;
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=1463844; DOI=10.1007/bf00028896;
RA Ellersiek U., Steinmueller K.;
RT "Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and
RT the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803.";
RL Plant Mol. Biol. 20:1097-1110(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
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).
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.
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 is composed of at least 11 different subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62517; CAA44374.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10885.1; -; Genomic_DNA.
DR PIR; S27972; QXYB1.
DR AlphaFoldDB; P26522; -.
DR SMR; P26522; -.
DR IntAct; P26522; 8.
DR STRING; 1148.1001395; -.
DR PaxDb; P26522; -.
DR EnsemblBacteria; BAA10885; BAA10885; BAA10885.
DR KEGG; syn:sll0519; -.
DR eggNOG; COG1005; Bacteria.
DR InParanoid; P26522; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; P26522; -.
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: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:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..372
FT /note="NAD(P)H-quinone oxidoreductase subunit 1"
FT /id="PRO_0000117520"
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..362
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 372 AA; 40548 MW; 4D9E02576825E990 CRC64;
MTSGIDLQNS FLQSLQGFGL PPGLAKLFWI PLPSILMIIG ATVGVLVVVW LERKISAAAQ
QRIGPEYAGP LGVLQPVADG IKLVFKEDVV PAKADPWLFT LGPVLVVLPV FLSYLIVPFG
QNLVITDINV GIFLWIALSS IAPIGLLMSG YASNNKYSLL GGLRAAAQSI SYEIPLSLAV
LAIVMMSNSL STIDIVDQQS GYGILGWNIW RQPVGFLIFW IAALAECERL PFDLPEAEEE
LVAGYQTEYA GMKFALFYLG SYVNLVLSAL VFSVLYLGGW DFPIPLENVA NWLGVAPTTS
WLQVLMAALG ITMTVLKSYF LIFIAILLRW TVPRVRIDQL LNLGWKFLLP VALANLLITA
ALKLTFPMAF GG
