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
//