ID K9ZE18_ANACC Unreviewed; 120 AA.
AC K9ZE18;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NAD(P)H dehydrogenase subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit 3 {ECO:0000256|HAMAP-Rule:MF_01394};
DE Short=NDH-C {ECO:0000256|HAMAP-Rule:MF_01394};
GN Name=ndhC {ECO:0000256|HAMAP-Rule:MF_01394};
GN OrderedLocusNames=Anacy_1973 {ECO:0000313|EMBL:AFZ57458.1};
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ57458.1, ECO:0000313|Proteomes:UP000010474};
RN [1] {ECO:0000313|Proteomes:UP000010474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|HAMAP-Rule:MF_01394}.
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:0000256|HAMAP-Rule:MF_01394};
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:0000256|HAMAP-Rule:MF_01394};
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:0000256|HAMAP-
CC Rule:MF_01394}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01394}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000256|ARBA:ARBA00008472, ECO:0000256|HAMAP-Rule:MF_01394}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01394}.
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DR EMBL; CP003659; AFZ57458.1; -; Genomic_DNA.
DR RefSeq; WP_015214106.1; NZ_AP018166.1.
DR AlphaFoldDB; K9ZE18; -.
DR STRING; 272123.Anacy_1973; -.
DR KEGG; acy:Anacy_1973; -.
DR PATRIC; fig|272123.3.peg.2150; -.
DR eggNOG; COG0838; Bacteria.
DR HOGENOM; CLU_119549_1_1_3; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000010474; Chromosome.
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; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 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; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR PANTHER; PTHR11058:SF9; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01394};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01394};
KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01394};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394};
KW Reference proteome {ECO:0000313|Proteomes:UP000010474};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01394};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01394}.
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ SEQUENCE 120 AA; 13688 MW; 1A18A519584793CA CRC64;
MFVLSGYEYL LGFFLLCSLV PALALSASKL LRPSSFSPER RTTYESGMEP IGGAWIQFNI
RYYMFALVFV VFDVETVFLY PWAVAFHRLG LLAFIEALVF IAILVIALVY AWRKGALEWS
//
