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NU4C2_SYNE7
ID   NU4C2_SYNE7             Reviewed;         534 AA.
AC   Q31LR3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 2 {ECO:0000255|HAMAP-Rule:MF_00491};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00491};
DE   AltName: Full=NAD(P)H dehydrogenase I, chain 4 2 {ECO:0000255|HAMAP-Rule:MF_00491};
DE   AltName: Full=NDH-1, chain 4 2 {ECO:0000255|HAMAP-Rule:MF_00491};
GN   Name=ndhD2 {ECO:0000255|HAMAP-Rule:MF_00491};
GN   OrderedLocusNames=Synpcc7942_1976;
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 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. {ECO:0000255|HAMAP-Rule:MF_00491}.
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_00491};
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_00491};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00491}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00491}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00491}.
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DR   EMBL; CP000100; ABB58006.1; -; Genomic_DNA.
DR   RefSeq; WP_011244430.1; NC_007604.1.
DR   AlphaFoldDB; Q31LR3; -.
DR   SMR; Q31LR3; -.
DR   STRING; 1140.Synpcc7942_1976; -.
DR   PRIDE; Q31LR3; -.
DR   EnsemblBacteria; ABB58006; ABB58006; Synpcc7942_1976.
DR   KEGG; syf:Synpcc7942_1976; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_0_3; -.
DR   OMA; ITRWGNQ; -.
DR   OrthoDB; 535707at2; -.
DR   BioCyc; MetaCyc:SYNPCC7942_1976-MON; -.
DR   BioCyc; SYNEL:SYNPCC7942_1976-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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
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; Thylakoid; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..534
FT                   /note="NAD(P)H-quinone oxidoreductase chain 4 2"
FT                   /id="PRO_0000343259"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ   SEQUENCE   534 AA;  58645 MW;  D94FEE71C4153AC2 CRC64;
     MEIGTFPWLT TIILLPIVAA LFIPLLPDRD GKGTTIRWYS LIVGLVDFIL LVVAFWTSYD
     FSNPDLQLVE SYAWVPQIGL NWSVGADGLS MPLILLTGFI STLAMLAAWP VTFKTRFFYF
     LMLAMYGGQI LVFAVQDLLV FFFAWELELI PVYLLLAIWG GKRRQYAATK FILYTAGSSL
     FILVASLAMA FSGDVISFDF QTLAAKEYAI GFQLLLYAGF LIAYGVKLPI VPLHTWLPDA
     HGEATAPVHM LLAGILLKMG GYALFRMNAG MLPEAHARFA PILVLLGVVN ILYAALTSFA
     QRNLKRKIAY SSISHMGFVL IGLGSFTQLG LSGSMLQMVS HGLIGASLFF LVGATYDRTH
     TLMLDEMGGV GQKMRKMFAM WTTCAMASLA LPGMSGFVAE LMVFVGFATS DAYGLPFKVV
     VISLAAIGVI LTPIYLLSML REIFFGPENK TLTEHETLVD AEPREVYIIA CLLVPIIGIG
     LYPKLTTQVY DATLVQLTER LRSAVPVIAQ QAEASRDRLS HFPGQAHRQA PPLG
 
 
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