ID A0A0T5P117_9RHOB Unreviewed; 631 AA.
AC A0A0T5P117;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:KRS14842.1};
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:QEW29955.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:QEW29955.1};
GN Name=nuoL_2 {ECO:0000313|EMBL:QEW29955.1};
GN ORFNames=RIdsm_05801 {ECO:0000313|EMBL:QEW29955.1}, XM52_26595
GN {ECO:0000313|EMBL:KRS14842.1};
OS Roseovarius indicus.
OG Plasmid pRIdsm_02 {ECO:0000313|EMBL:QEW29955.1}, and
OG Plasmid pridsm_02 {ECO:0000313|Proteomes:UP000325785}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS14842.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS14842.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS14842.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW29955.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW29955.1,
RC ECO:0000313|Proteomes:UP000325785};
RC PLASMID=pridsm_02 {ECO:0000313|Proteomes:UP000325785}, and pRIdsm_02
RC {ECO:0000313|EMBL:QEW29955.1};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-2018) 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; LAXI01000032; KRS14842.1; -; Genomic_DNA.
DR EMBL; CP031600; QEW29955.1; -; Genomic_DNA.
DR RefSeq; WP_009827255.1; NZ_LAXI01000032.1.
DR AlphaFoldDB; A0A0T5P117; -.
DR STRING; 540747.SAMN04488031_11789; -.
DR KEGG; rid:RIdsm_05801; -.
DR PATRIC; fig|540747.5.peg.4082; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; Plasmid pridsm_02.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
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.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:QEW29955.1};
KW Plasmid {ECO:0000313|EMBL:QEW29955.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051401};
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..21
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..105
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 121..402
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 631 AA; 64512 MW; 95439B1D2D4CD10F CRC64;
MTMLALIILA PLLAGLAELV LRRAPEAIAL VGVGIGFLAA MGTLAGAVAG DAVQLVLPGL
PQKPLRLVAV PLTAVFSAMV ATVAACVLVY AVGYMRSDPE RPRFFGIVLL FVAAMQALVL
AGDWITVLAA WELIGFSSYL LIGFWHGRDG VPSAATRAFL YTRSADLGLY LGIFVLIGWA
GTSEISATLA ISGTPALVAG LLLLVGAMGK SAQVPLQDWL QRAMAGPTPV SALLHSATLV
AAGAILLIRV APMLPAGALI AVGLVGGVTA VVTGLIALAE RDLKRLLAAS TSSQYGLMLL
AIGAGVPVAA LLHLIAHAAI KSTLFLGAGV FQHDRDSTDM DAVAGAGRAR PLVLSAFAVA
AVALAGIPPL AGFFSKDAIL AAALAAPGVV WLAPLALAGT VLTGAYMARA LRVLWQGEAQ
PVLGKGMGWM GAGMAVLTAL AAGLGFAFTP LEHLLEAKLP PEGPAMILGL VAALSGLLLG
WFVAPTRLMG PVLPMAQRGF AVAGGMDGLV LRPALAFAAA CEGFERRLLA AQLGLVRILS
LGTASSAERS DNRLYAATLQ VGRMNLRLGD GAENTDTHGI DGLIFGLVAR TIAAGRRLRL
LQSGLIHREL ALTVMGIAVI AAVLLILPMS S
//
