ID A0A1H8N9H8_9RHOB Unreviewed; 680 AA.
AC A0A1H8N9H8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:SEO26217.1};
GN ORFNames=SAMN04490248_10368 {ECO:0000313|EMBL:SEO26217.1};
OS Salinihabitans flavidus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salinihabitans.
OX NCBI_TaxID=569882 {ECO:0000313|EMBL:SEO26217.1, ECO:0000313|Proteomes:UP000198893};
RN [1] {ECO:0000313|EMBL:SEO26217.1, ECO:0000313|Proteomes:UP000198893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27842 {ECO:0000313|EMBL:SEO26217.1,
RC ECO:0000313|Proteomes:UP000198893};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
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}.
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DR EMBL; FODS01000003; SEO26217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8N9H8; -.
DR STRING; 569882.SAMN04490248_10368; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000198893; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
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; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
DR PRINTS; PR01435; NPOXDRDTASE5.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198893};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..109
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 135..440
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 680 AA; 74868 MW; 588BFDF424B2D218 CRC64;
METIILFAPL VGAIIAGFGW RVIGEVAAQW VTTGLLFLAC LLSWIVFLGH DGVTEQIQIL
RWIESGTFQS DWAIRLDRLT AIMLIVVTTV SALVHLYSFG YMAHDENFRE HESYKPRFFA
YLSFFTFAML MLVTSDNLVQ MFFGWEGVGV ASYLLIGFYY RKPSANAAAI KAFVVNRVGD
FGFALGIAGL FFLVDSVRLD DIFAAGPMLA ETQVAFLWTE WNAANLLAFL LFVGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LFEYAPEALI FVTFIGATTA
FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGVGVYSVA MFHLFTHAFF KAMLFLGAGS
VIHGMHHEQD MRNYGGLRKK LPYTFWAMMI GTLAITGVGI PLTQIGFAGF LSKDAVIESA
WAGTAGGYAF WMLVIAALFT SFYSWRLMFL TFFGEARGNK KTHDHAHESP MVMIAPLGVL
ALGAVFSGMI WYGSFFGDHD QVNRFFGIPE HHAEASDDTA EAGDAAAMTA PQGAIFMAPD
NHVMDDAHHA PTWVKVSPFI AMLIGLAVAY LFYIVNTSLP RRLAEAQRPL YLFLLNKWYF
DEAYDVIFVR PAKSLGRLLW KRGDGSVIDG FLNGVAMGII PFFTRLAGRA QSGYIFTYAF
AMVLGIAILI TWITLSGGAN
//
