ID F0UWE1_AJEC8 Unreviewed; 508 AA.
AC F0UWE1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404};
DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003404};
GN ORFNames=HCEG_12004 {ECO:0000313|EMBL:EGC40626.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OG Mitochondrion {ECO:0000313|EMBL:EGC40626.1}.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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:RU003404}.
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:RU003404};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC {ECO:0000256|RuleBase:RU003404}.
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DR EMBL; DS990652; EGC40626.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UWE1; -.
DR STRING; 544711.F0UWE1; -.
DR HOGENOM; CLU_007100_6_0_1; -.
DR OMA; FWFTRIA; -.
DR Proteomes; UP000008142; Mitochondrion.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00361; Proton_antipo_M; 2.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404};
KW Mitochondrion {ECO:0000256|RuleBase:RU003404, ECO:0000313|EMBL:EGC40626.1};
KW NAD {ECO:0000256|RuleBase:RU003404};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003404};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003404}; Transport {ECO:0000256|RuleBase:RU003404};
KW Ubiquinone {ECO:0000256|RuleBase:RU003404}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 253..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 361..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT DOMAIN 1..30
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 46..158
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 159..266
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 508 AA; 56899 MW; D087832B2863C551 CRC64;
MLIPVLIVSS LVHIYSIGYM SHDPHNQRFF SYLSLFTFMM IILVTANNYL LMFLGWEGVG
VCSYLLINFW FTRIAANQSS ISAFLTNRVG DCFLMIGMFI IIWSFGNINY STIFSLAPYL
NSNIITLIGI CLLIGAMAKS SQIGLHVWLP QAMEGPTPQL GMMVIAIGLS SYNIALFHLV
NHAFYKALLF LGAGAIIHSV SDNQDFRKFG GLKAFLPLTY SVMLIASLSL VAIPFMTGFY
SKDFILESAY GQFYLSSIIV YILASVGAIF TTLYSAKVLY LTFLTNPNGP LITYKKADQG
DLFINLPLII LAILSIFFGY LTKDLFIGLG TGFFSDNSLF IHPLHESMLD TEFAVITLFK
LLPFILTISL SFLSLLLSEF FGLFVIKFKY TKLGYNLFGF FNQRFLIELF YNNYITDIVL
KLGGQTTKII DKGSVELLGP YGLEKSLLVL SNGIGNLSTG IITSYGLYIL IGFFSYISLF
YFSFIDGNIL LLLLIAIFTI FNKTYNEN
//