(data stored in ACNUC5340 zone)

SWISSPROT: NU3C_ACAM1

ID   NU3C_ACAM1              Reviewed;         120 AA.
AC   B0C6C4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
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=AM1_0132;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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}.
DR   EMBL; CP000828; ABW25218.1; -; Genomic_DNA.
DR   RefSeq; WP_010469000.1; NC_009925.1.
DR   SMR; B0C6C4; -.
DR   STRING; 329726.AM1_0132; -.
DR   PRIDE; B0C6C4; -.
DR   EnsemblBacteria; ABW25218; ABW25218; AM1_0132.
DR   KEGG; amr:AM1_0132; -.
DR   eggNOG; ENOG4105KWU; Bacteria.
DR   eggNOG; COG0838; LUCA.
DR   HOGENOM; HOG000100120; -.
DR   KO; K05574; -.
DR   OMA; RFPVKYY; -.
DR   OrthoDB; 1748431at2; -.
DR   Proteomes; UP000000268; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C: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;
DR   PRODOM; B0C6C4.
DR   SWISS-2DPAGE; B0C6C4.
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..120
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 3"
FT                   /id="PRO_0000362608"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   120 AA;  13492 MW;  E78DB8242301AE7F CRC64;
     MFALSGYEYL LGFLLLCSLV PALALSASKV LRPSNQGAVR RTTYESGMEP VGGAWIQFNI
     RYYMFALVFV IFDVETVFLY PWAVAFHKLG VLAFIEALIF IAILIVGLVY AWRKGALEWS
//

If you have problems or comments...

PBIL Back to PBIL home page