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NU4C_MARPO
ID   NU4C_MARPO              Reviewed;         499 AA.
AC   P06263;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 4, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase, chain 4;
DE   AltName: Full=NADH-plastoquinone oxidoreductase chain 4;
GN   Name=ndhD; Synonyms=ndh4;
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3199437; DOI=10.1016/0022-2836(88)90004-6;
RA   Kohchi T., Shirai H., Fukuzawa H., Sano T., Komano T., Umesono K.,
RA   Inokuchi H., Ozeki H., Ohyama K.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   IV. Inverted repeat and small single copy regions.";
RL   J. Mol. Biol. 203:353-372(1988).
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: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; X04465; CAA28134.1; -; Genomic_DNA.
DR   PIR; A00445; DELVN4.
DR   RefSeq; NP_039348.1; NC_001319.1.
DR   AlphaFoldDB; P06263; -.
DR   SMR; P06263; -.
DR   GeneID; 2702577; -.
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   Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..499
FT                   /note="NAD(P)H-quinone oxidoreductase chain 4,
FT                   chloroplastic"
FT                   /id="PRO_0000118018"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
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        211..231
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        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   499 AA;  56667 MW;  81F5BB4011D6A629 CRC64;
     MNHFPWLTII VLFPISAGLV IPFLPSTGNK IIRWYTLGVC LLEFLLITYI FCYHYQFNDH
     LIQLKEDYNW ISFINFHWRL GIDGFSIGLI LLTGFITTLA TLAAWPVTRN PRLFYFLMLA
     MYSGQIGLFA SQDILLFFFM WELELLPVYL LLAMWGGKRR LYAATKFILY TAAGSLFILI
     GGLIMAFYNS NEFTFDFQFL INKKYPLELE IIIYLSFLIA YAVKLPIIPF HTWLPDTHGE
     AHYSTCMLLA GILLKMGAYG LIRINMELLP HAHSFFAPWL VIVGAIQIVY AALTSLSQRN
     LKRRIAYSSV SHMGFVLIGI GSITNLGLNG AILQMISHGL IGASLFFLAG ISYDRTRTLV
     LDQMGGIGNS MPKIFTLFTS CSMASLALPG MSGFIAELMI FLGVIDNPNY SSLFKIIIII
     IQGIGIILTP IYLLSMLRQM FYGYKFSNTL EPYFMDAGPR EIFILICLFF PIISIGIYPN
     FVLSIWNSKV NFLLSNNFF
 
 
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