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
//