NU4C2_SYNY3
ID NU4C2_SYNY3 Reviewed; 559 AA.
AC P72823; Q55021;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4-2;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase I, subunit D-2;
DE AltName: Full=NDH-1, chain 4-2;
GN Name=ndhD2; OrderedLocusNames=slr1291;
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=7846157; DOI=10.1104/pp.106.4.1435;
RA Dzelzkalns V.A., Obinger C., Regelsberger G., Niederhauser H., Kamensek M.,
RA Peschek G.A., Bogorad L.;
RT "Deletion of the structural gene for the NADH-dehydrogenase subunit 4 of
RT Synechocystis 6803 alters respiratory properties.";
RL Plant Physiol. 106:1435-1442(1994).
RN [2]
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 NAD(P)H, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox 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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85105.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14130; AAA85105.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000022; BAA16838.1; -; Genomic_DNA.
DR PIR; S74687; S74687.
DR PIR; T14239; T14239.
DR AlphaFoldDB; P72823; -.
DR SMR; P72823; -.
DR IntAct; P72823; 2.
DR STRING; 1148.1651912; -.
DR PaxDb; P72823; -.
DR EnsemblBacteria; BAA16838; BAA16838; BAA16838.
DR KEGG; syn:slr1291; -.
DR eggNOG; COG1008; Bacteria.
DR InParanoid; P72823; -.
DR OMA; QSNMKRR; -.
DR PhylomeDB; P72823; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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:0048039; F:ubiquinone binding; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR HAMAP; MF_00491; NDH1_NuoM; 1.
DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="NAD(P)H-quinone oxidoreductase chain 4-2"
FT /id="PRO_0000118036"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 64
FT /note="Q -> I (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..110
FT /note="DH -> TS (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..121
FT /note="LV -> VL (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> S (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..130
FT /note="GVF -> VLI (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="M -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> LS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="CI -> VS (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..184
FT /note="AL -> P (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="A -> S (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..227
FT /note="AGLLIAFGVKLAI -> TGLALVAFAVKISH (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..301
FT /note="DNM -> AH (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..332
FT /note="GIASFTDLGISGAM -> LFSITIGIMDH (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> R (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..349
FT /note="LA -> PWT (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="H -> N (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> P (in Ref. 1; AAA85105)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="Q -> QE (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61007 MW; 168DD5302A8810A3 CRC64;
MLEHFPWLTT MIALPLVAAL FIPLIPDKDG KQVRWYALGV GLADFVLMSY VFWTNYDISS
TGFQLQEKFS WIPQFGLSWS VSVDGISMPL VLLAGLVTTL SIFAAWQVDH KPRLFYFLML
VLYAAQIGVF VAQDMLLLFI MWELELVPVY LLVCIWGGQK RQYAAMKFLL YTAAASVFIL
VAALGLAFYG DVTTFDIAEL GLKDYPIALE LFLYAGLLIA FGVKLAIFPF HTWLPDAHGE
ASAPVSMILA GVLLKMGGYG LIRLNLGLLE DAHVYFAPIL VILGVVNIIY GGFSSFAQDN
MKRRLAYSSV SHMGFVLLGI ASFTDLGISG AMLQMLSHGL IAAVLFFLAG VTYDRTHTLS
LAQMGNIGKV MPTVFALFTM GAMASLALPG MSGFVSELAV FVGVSSSDIY STPFKTVTVF
LAAVGLVLTP IYLLSMLRQL FYGNNIPPSC NLEQDNLSAN SDQEAVCFGT SCVLPGNAIY
DDARPREVFI AACFLLPIIA VGLYPKLATQ TYDATTVAVN SQVRQSYVQI AETNPRVYAE
ALTAPHIPTT DFATVKVQP
