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Database: UniProt
Entry: Q1XGB5_PHYPA
LinkDB: Q1XGB5_PHYPA
Original site: Q1XGB5_PHYPA 
ID   Q1XGB5_PHYPA            Unreviewed;       495 AA.
AC   Q1XGB5;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4 {ECO:0000256|RuleBase:RU003297};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU003297};
GN   Name=nad4 {ECO:0000313|EMBL:BAE93089.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG   Mitochondrion {ECO:0000313|EMBL:BAE93089.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:BAE93089.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=17175527; DOI=10.1093/molbev/msl198;
RA   Terasawa K., Odahara M., Kabeya Y., Kikugawa T., Sekine Y., Fujiwara M.,
RA   Sato N.;
RT   "The mitochondrial genome of the moss Physcomitrella patens sheds new light
RT   on mitochondrial evolution in land plants.";
RL   Mol. Biol. Evol. 24:699-709(2007).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000256|RuleBase:RU003297}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU003297};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       membrane {ECO:0000256|RuleBase:RU003297}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003297}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC       {ECO:0000256|ARBA:ARBA00009025, ECO:0000256|RuleBase:RU003297}.
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DR   EMBL; AB251495; BAE93089.1; -; Genomic_DNA.
DR   RefSeq; YP_539018.1; NC_007945.1.
DR   STRING; 3218.Q1XGB5; -.
DR   GeneID; 3989057; -.
DR   KEGG; ppp:3989057; -.
DR   eggNOG; KOG4845; Eukaryota.
DR   InParanoid; Q1XGB5; -.
DR   OrthoDB; 1946151at2759; -.
DR   Proteomes; UP000006727; Mitochondrion.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0009536; C:plastid; IEA:UniProt.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
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   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   NCBIfam; TIGR01972; NDH_I_M; 1.
DR   PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR   PANTHER; PTHR43507:SF19; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU003297};
KW   Membrane {ECO:0000256|RuleBase:RU003297};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003297, ECO:0000313|EMBL:BAE93089.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003297};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Respiratory chain {ECO:0000256|RuleBase:RU003297};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|RuleBase:RU003297};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003297};
KW   Transport {ECO:0000256|RuleBase:RU003297};
KW   Ubiquinone {ECO:0000256|RuleBase:RU003297}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        82..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        143..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        173..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        275..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        334..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        368..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        411..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   TRANSMEM        455..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003297"
FT   DOMAIN          138..419
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   495 AA;  56248 MW;  16EA39C5B9F72386 CRC64;
     MLQFLAPFYS NLSGLILCPL LGSIILFVIP DPRIRLIRSI GLCTSLITFL YSLLFWIQFD
     NSTAKFQFVE TIRWLPYSNI NFYIGIDGIS SFFVVLTTFL IPICILVGWS SIKSYKKEYM
     IAFLILESFM IAVFCMLDLL LFYVFFESVL IPMFIIIGVW GSRQRKIQAA YQFFLYTLLG
     SVFMLLAILF IFFQTGTTDL QILLTTEFSE RRQILLWIAF FASFSVKVPM IPVHIWLPEA
     HVEAPTAGSV ILAGILLKLG TYGFLRFSIP MFPEATLXFT PFIYTLSVIA IIYTSLTTIR
     QIDLKKIIAY SSVAHMNFVT IGMFSLNIQG IEGSILLMLS HGLVSSALFL CVGVLYDRHK
     TRLVKYYGGL VSTMPMFSTI FLFFTLANMS LPGTSSFIGE FLILVGAFQR NSLVATLAAL
     GMILGAAYSL WLYNRVIFGN FKPKFLQKFS DLNRREVLIF FPFIVGVIWM GVYPEVFLEC
     MHTSVSNLVQ HGKFD
//
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