NU1C_SYNE7
ID NU1C_SYNE7 Reviewed; 372 AA.
AC Q31NJ6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NAD(P)H dehydrogenase I subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-1 subunit 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-A {ECO:0000255|HAMAP-Rule:MF_01350};
GN Name=ndhA {ECO:0000255|HAMAP-Rule:MF_01350};
GN OrderedLocusNames=Synpcc7942_1343;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01350}.
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_01350};
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_01350};
CC -!- SUBUNIT: NDH-1 is composed of at least 11 different subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR EMBL; CP000100; ABB57373.1; -; Genomic_DNA.
DR RefSeq; WP_011242524.1; NC_007604.1.
DR AlphaFoldDB; Q31NJ6; -.
DR SMR; Q31NJ6; -.
DR STRING; 1140.Synpcc7942_1343; -.
DR PRIDE; Q31NJ6; -.
DR EnsemblBacteria; ABB57373; ABB57373; Synpcc7942_1343.
DR KEGG; syf:Synpcc7942_1343; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_3; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1343-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1343-MON; -.
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: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; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..372
FT /note="NAD(P)H-quinone oxidoreductase subunit 1"
FT /id="PRO_0000240048"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 372 AA; 40364 MW; 916B0D93F76F19F7 CRC64;
MDRGIDLQGT FIQSLESLGL SPGLSKVLWM PLPMLLMIIA ATVGVLVTVW LERKISAAVQ
QRIGPEYAGP LGVLQSAADG LKLILKEDII PAKADAFLFT IGPALVVIPV FLSYLIVPFG
QELIITNVGA GVFLWIALSS IQPIGLLMSG YASNNKYSLL GGLRAAAQSI SYEIPLALAV
LAVVMMSNSL STIDIVDQQS GYGILGWNIW RQPVGFIIFW IAALAECERL PFDLPEAEEE
LVAGYQTEYA GMKFALFYVG SYVNLILSAL LVSILYLGGW EFPIPLDRVA DWIGVDPANP
ILQITTAALG ITMTVLKAYL LVFTAILLRW TVPRVRIDQL LDLGWKFLLP ISLVNLLVTA
ALKLTFPVAF GG
