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NU4C_LOBMA
ID   NU4C_LOBMA              Reviewed;         500 AA.
AC   A4QLP7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 4, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00491};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00491};
DE   AltName: Full=NAD(P)H dehydrogenase, chain 4 {ECO:0000255|HAMAP-Rule:MF_00491};
DE   AltName: Full=NADH-plastoquinone oxidoreductase chain 4 {ECO:0000255|HAMAP-Rule:MF_00491};
GN   Name=ndhD {ECO:0000255|HAMAP-Rule:MF_00491};
OS   Lobularia maritima (Sweet alyssum) (Alyssum maritimum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Anastaticeae; Lobularia.
OX   NCBI_TaxID=226051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Lobularia maritima chloroplast DNA.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00491}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00491}.
CC   -!- RNA EDITING: Modified_positions=1 {ECO:0000250}; Note=The initiator
CC       methionine is created by RNA editing. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00491}.
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DR   EMBL; AP009375; BAF50602.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; YP_001123777.2; NC_009274.1.
DR   AlphaFoldDB; A4QLP7; -.
DR   SMR; A4QLP7; -.
DR   GeneID; 4964885; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="NAD(P)H-quinone oxidoreductase chain 4,
FT                   chloroplastic"
FT                   /id="PRO_0000343290"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        113..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ   SEQUENCE   500 AA;  56034 MW;  8FDC50BC0A5547F0 CRC64;
     MNDFPWLTII VVFPISAGSL MLFLPHRGNK VNKWYTICIS ILELLLTTYA FCYNFKMDDP
     LIQLSEDYKW INFFDFYWRL GIDGLSIGTI LLTGFITTLA TLAAFPVTRN SRLFHFLMLA
     MYSGQIGLFS SRDLLLFFIM WELELIPVYL LLSMWGGKKR LYSATKFILY TAGSSIFLLI
     GVLGISLYGS NEPTLNLELL ANQSYPVTLE ILLYIGFLIA FAVKLPIIPF HTWLPDTHGE
     AHYSTCMLLA GILLKMGAYG LVRINMELLP HAHSMFSPWL MVVGTIQIIY AASTSPGQRN
     LKKRIAYSSV SHMGFIIIGI GSITDPGLNG AILQIISHGF IGAALFFLAG TSYDRIRLGY
     LDEMGGMAIS IPKIFTMFTI LSMASLALPG MSGFVAELIV FFGIITSQKY FLISKILIIF
     VMAIGMILTP IYLLSMSRQM FYGYKLINVK NFSFFDSGPR ELFLSISILL PIIGIGIYPD
     FVLSLASDKV ESILSNYFYG
 
 
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