ID A0A1I6CNQ3_9RHOB Unreviewed; 703 AA.
AC A0A1I6CNQ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:SFQ94794.1};
GN ORFNames=SAMN04515673_10198 {ECO:0000313|EMBL:SFQ94794.1};
OS Poseidonocella sedimentorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871652 {ECO:0000313|EMBL:SFQ94794.1, ECO:0000313|Proteomes:UP000199302};
RN [1] {ECO:0000313|EMBL:SFQ94794.1, ECO:0000313|Proteomes:UP000199302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC {ECO:0000313|Proteomes:UP000199302};
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; FOYI01000001; SFQ94794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6CNQ3; -.
DR STRING; 871652.SAMN04515673_10198; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000199302; 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:UP000199302};
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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..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 579..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..698
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"
FT REGION 517..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 77246 MW; 7D2D3D36318B9706 CRC64;
MEQIILFAPL LGALIGGFGW KTIGEAGAMW VTTGLLFLSA LLSWIVFLGF DGQTQQIHLL
DWIQSGTLDT SWAIRLDRLT AIMLVVITTV SALVHLYSFG YMAGDPQWRE GEVYRPRFFA
YLSFFTFAML MLVTADNLVQ MFFGWEGVGV ASYLLIGFYW RKPSANGAAI KAFVVNRVGD
FGFALGIFAL FFLVDSVNLD DIFAAGPALA ETDLRFLWRD WVAVEVIAVL LFIGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LMEYAPAATG FITLIGATTA
FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGVGVYSVA MFHLFTHAFF KAMLFLGAGS
VIHAMHHEQD MRNYGGLRRK IPYTFWAMLI GTLAITGVGI PLTHIGFAGF LSKDAVIESA
WAGTSGGYAF WMLVIAALFT SFYSWRLMFL TFWGKPRGDK QTHKHAHESP MVMLVPLGVL
ALGAVFSGMI WYGSFFGEHA QVNRFFGIPD AHAEAAEAGH ADAEDHAGAE TGAEVSAETG
AETEPHAVPQ GYAPEGAIFM APDNHVLDDA HHAPKWVKLS PFIAMVLGFL VAVWFYILNP
KLPKLVAQSQ RPLYYFLLNK WYFDELYGFL FVRPAYALGR LFWKQGDGAL INGAINGLAM
GIIPFFTRLA GRAQSGYIFT YVFWMVVGIA VLITWMSLAG GDR
//