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NU4C1_SYNY3
ID   NU4C1_SYNY3             Reviewed;         525 AA.
AC   P32421;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 4-1;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase I, subunit D-1;
DE   AltName: Full=NDH-1, chain 4-1;
GN   Name=ndhD1; Synonyms=ndhD; OrderedLocusNames=slr0331;
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=1463844; DOI=10.1007/bf00028896;
RA   Ellersiek U., Steinmueller K.;
RT   "Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and
RT   the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803.";
RL   Plant Mol. Biol. 20:1097-1110(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [3]
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}.
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DR   EMBL; X65170; CAA46289.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA10037.1; -; Genomic_DNA.
DR   PIR; S28891; S28891.
DR   AlphaFoldDB; P32421; -.
DR   SMR; P32421; -.
DR   IntAct; P32421; 4.
DR   STRING; 1148.1001415; -.
DR   PaxDb; P32421; -.
DR   EnsemblBacteria; BAA10037; BAA10037; BAA10037.
DR   KEGG; syn:slr0331; -.
DR   eggNOG; COG1008; Bacteria.
DR   InParanoid; P32421; -.
DR   OMA; ITRWGNQ; -.
DR   PhylomeDB; P32421; -.
DR   Proteomes; UP000001425; Chromosome.
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; Reference proteome; Thylakoid;
KW   Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..525
FT                   /note="NAD(P)H-quinone oxidoreductase chain 4-1"
FT                   /id="PRO_0000118035"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   525 AA;  57511 MW;  CC478354466E7DF9 CRC64;
     MNTFPWLTTI ILLPIVAALF IPIIPDKDGK TVRWYSLAVG LVDFALIVYA FYSGFDLSEP
     GLQLVESYTW LPQIDLKWSV GADGLSMPLI ILTGFITTLA TMAAWPVTLK PKLFYFLMLL
     MYGGQIAVFA VQDILLFFLV WELELVPVYL ILSIWGGKKR LYAATKFILY TAGGSLFILL
     AGLTLAFYGD VNTFDMSAIA AKDIPVNLQL LLYAGFLIAY GVKLPIFPLH TWLPDAHGEA
     TAPAHMLLAG ILLKMGGYAL LRMNVGMLPD AHAVFAPVLV ILGVVNIIYA AFTSFAQRNL
     KRKIAYSSIS HMGFVLIGLA SFTDLGMSGA MLQMISHGLI GASLFFMVGA TYDRTHTLML
     DEMGGIGQKM KKGFAMWTAC SLASLALPGM SGFVAELMVF VGFATSDAYN LVFRTIVVVL
     MGVGVILTPI YLLSMLREML YGPENEELVN HTNLVDVEPR EVFIIGCLLV PIIGIGFYPK
     LITQIYDPTI NQLVQTARRS VPSLVQQANL SPLEVTALRP PTIGF
 
 
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