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Database: UniProt
Entry: A0A2A8HWJ1_9SPHN
LinkDB: A0A2A8HWJ1_9SPHN
Original site: A0A2A8HWJ1_9SPHN 
ID   A0A2A8HWJ1_9SPHN        Unreviewed;       696 AA.
AC   A0A2A8HWJ1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=NADH:ubiquinone reductase (H(+)-translocating) {ECO:0000256|ARBA:ARBA00012944};
DE            EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944};
GN   ORFNames=B2G71_08140 {ECO:0000313|EMBL:PEQ13388.1};
OS   Novosphingobium sp. PC22D.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ13388.1, ECO:0000313|Proteomes:UP000220675};
RN   [1] {ECO:0000313|EMBL:PEQ13388.1, ECO:0000313|Proteomes:UP000220675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC22D {ECO:0000313|EMBL:PEQ13388.1,
RC   ECO:0000313|Proteomes:UP000220675};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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:PEQ13388.1}.
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DR   EMBL; MWMO01000003; PEQ13388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8HWJ1; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000220675; 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   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:UP000220675};
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        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        383..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        521..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        577..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        676..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..117
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          133..429
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          567..688
FT                   /note="NADH dehydrogenase subunit 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06455"
FT   REGION          471..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  75669 MW;  37DC9B99C1C3FCB5 CRC64;
     MHPILIIVFL PLLAAIAAGL GNKQLGATTA KILTTGALFV SCVLSWPIFL GFVAGGAEAS
     VVPVLKWVES GAMTFDWALR VDSLTAVMLV VITTVSALVH LYSWGYMDED PDQPRFFAYL
     SLFTFAMLML VTADNLVQMF FGWEGVGLAS YLLIGFWFRK PSACAAAIKA FVVNRVGDLG
     FMLGIFGTFL VFGTTSIPEI LAAAPGMAGS TIGFLGYRFD TMTVLCILLF IGAMGKSAQL
     GLHTWLPDAM EGPTPVSALI HAATMVTAGV FMVCRLSPMF EASPSAMAFV AVIGGATCFF
     AATIGCTQWD IKRVIAYSTC SQLGYMFFAA GVGAYGAAMF HLFTHAFFKA LLFLGAGSVI
     HAMHHEQDMR YYGALRKEIP ITFWTMTAGT LAITGVGIAG FVGFAGFYSK DAILEAAFGA
     GTQVGQFAFW MGILAALMTS FYSWRLVFLT FFGKPRWAAS EHIQHALHDE HGHDAHDTHG
     HGHEAENAPA QEDAGHDAAH SAHAADAHEG TGGYHPHESP LVMLIPLLVL SLGAVFAGFV
     FQHAFVSEGT GEFWQGALVF HEHLIHAMHE VPTWVKWSPF TVMAIGFVTA WYGYIRNTEF
     PAAVARQLGP VYTFVFRKWM FDELYHYVFV VPAFWLGRVF WKRGDEGTIN RFGPDGAAWV
     VARGATYAQK VQSGYLYSYA LVMLLGLVAA VSWVIK
//
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