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NU3C_TRIEI
ID   NU3C_TRIEI              Reviewed;         135 AA.
AC   Q10YT3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NDH-1 subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
DE            Short=NDH-C {ECO:0000255|HAMAP-Rule:MF_01394};
GN   Name=ndhC {ECO:0000255|HAMAP-Rule:MF_01394}; OrderedLocusNames=Tery_3501;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_01394}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01394}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01394}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01394}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG52591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000393; ABG52591.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q10YT3; -.
DR   SMR; Q10YT3; -.
DR   STRING; 203124.Tery_3501; -.
DR   EnsemblBacteria; ABG52591; ABG52591; Tery_3501.
DR   KEGG; ter:Tery_3501; -.
DR   eggNOG; COG0838; Bacteria.
DR   HOGENOM; CLU_119549_1_1_3; -.
DR   OMA; RFPVKYY; -.
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   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..135
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 3"
FT                   /id="PRO_0000362796"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   135 AA;  15735 MW;  091801B162E84AB7 CRC64;
     MFNRESYLLR KYRLIVFFLS GYEYFLGFLM ISSLVPIIAL TASKLLRPKT RGPERRTTYE
     SGVEPIGGAW IQFNIRYYMF ALVFVIFDVE TVFLYPWAVA FHQLGLLAFI EALIFIAILV
     VALVYAWRKG ALEWS
 
 
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