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Database: UniProt
Entry: A0A317EEQ3_9PROT
LinkDB: A0A317EEQ3_9PROT
Original site: A0A317EEQ3_9PROT 
ID   A0A317EEQ3_9PROT        Unreviewed;       660 AA.
AC   A0A317EEQ3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=NADH:ubiquinone reductase (H(+)-translocating) {ECO:0000256|ARBA:ARBA00012944};
DE            EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944};
GN   ORFNames=DKG75_04655 {ECO:0000313|EMBL:PWR23853.1};
OS   Zavarzinia compransoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Zavarziniaceae; Zavarzinia.
OX   NCBI_TaxID=1264899 {ECO:0000313|EMBL:PWR23853.1, ECO:0000313|Proteomes:UP000246077};
RN   [1] {ECO:0000313|Proteomes:UP000246077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1231 {ECO:0000313|Proteomes:UP000246077};
RA   Lee Y., Jeon C.O.;
RT   "Zavarzinia sp. HR-AS.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000766};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWR23853.1}.
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DR   EMBL; QGLF01000001; PWR23853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317EEQ3; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000246077; Unassembled WGS sequence.
DR   GO; GO:0070469; C:respirasome; 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   Gene3D; 1.20.5.2700; -; 1.
DR   InterPro; IPR010934; NADH_DH_su5_C.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   NCBIfam; TIGR01974; NDH_I_L; 1.
DR   PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   Pfam; PF06455; NADH5_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
DR   PRINTS; PR01435; NPOXDRDTASE5.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246077};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000320};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        634..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..114
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          131..421
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          527..649
FT                   /note="NADH dehydrogenase subunit 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06455"
SQ   SEQUENCE   660 AA;  72193 MW;  1091BDCBF83D7891 CRC64;
     MIAAIVFLPL LGAVIAGFFG RLIGARGAQI VTSTLLVVAA VLSWVTFFQV TGHEGGAYKM
     RLMTWVLSGA FEVDWAFRVD TLTAVMLVVV TSVSSLVHIY SVGYMAEDPH IPRFHAYLSL
     FTFAMLMLVT ADNFLQVFFG WEGVGLASYL LIGFWYKKPS ANAAAIKAFV VNRVGDFGFA
     LGIFAIFLVF NSVSFDTVFA AAAGKAGQTF NFLGYDVDIM TTICLLLFVG CMGKSAQLGL
     HTWLPDAMEG PTPVSALIHA ATMVTAGVFL VARASPLFEF APSALAVVTV VGATTAFFAA
     TVGLVQNDIK RVIAYSTCSQ LGYMFFAAGV GAYEAAVFHL FTHAFFKALL FLGAGSVIHA
     MHHEQDMRNM GGTWKYIKFT YAMMWIGNLA LAGVPFFAGF YSKDMVLEVA YAAHSGVGTY
     AFWLGIIAAS FTAFYSWRLL FLTFHGEKRW GGHGHGHGHD DHGHGHGHAH TPHESPLAMT
     IPLALLAVGA VFSGFWFYDS FVGEHREAFW GGAIFVAEAN KVIEHAHHVP GWVKLLPLIV
     TAGGIFVAWV FYILKPKWPD QLAKTHREAY AFLLNKWYFD ELYDLLFVKG ARLFGRVFWK
     QGDGAVIDGL GPNGISARVL DIARRAAKLQ SGFVYHYAFA MLIGVALLVT WYVYRMGVTP
//
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