ID Q05RG2_9SYNE Unreviewed; 626 AA.
AC Q05RG2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:EAU73318.1};
GN ORFNames=RS9916_27444 {ECO:0000313|EMBL:EAU73318.1};
OS Synechococcus sp. RS9916.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU73318.1, ECO:0000313|Proteomes:UP000004972};
RN [1] {ECO:0000313|EMBL:EAU73318.1, ECO:0000313|Proteomes:UP000004972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9916 {ECO:0000313|EMBL:EAU73318.1,
RC ECO:0000313|Proteomes:UP000004972};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox energy in a proton gradient. {ECO:0000256|ARBA:ARBA00025624}.
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 -!- 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:EAU73318.1}.
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DR EMBL; AAUA01000003; EAU73318.1; -; Genomic_DNA.
DR RefSeq; WP_007097426.1; NZ_DS022299.1.
DR AlphaFoldDB; Q05RG2; -.
DR STRING; 221359.RS9916_27444; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_3_3; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000004972; 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; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR010217; NU5C2.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01960; ndhF3_CO2; 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000004972};
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 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..138
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 154..439
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 626 AA; 67591 MW; 221D7E3968A9E111 CRC64;
MRWFRSCSRH LLLISDLTFA EQTSWLIPLY GFTGMVLALP WAAGWFRRDA HRPAAYLNIL
LTLLAFVHGS LVLQDVMALG PATLHYPWLS VVDLQLDISF SLSLTNVAAL ELITGLSLVS
QIYSLGYMDK EWALARFFAL LGFFEGAMSG VVLSDTLFQS YFLLEMLTLS TYLLVGFWYA
QPLVITAARD AFLTKRVGDV LLLMGVVALA AYAGVMGFDD LYAWAAEDKL SPLATTLIGL
GLIAGPMGKC AQFPMHLWLD EAMEGPNPAS ILRNSVVVTC GAIVLLKVMP LLQHAPVTLV
VLQVVGAISA IGGSLVSIAQ VDIKRTLSYS TTAYLGLVFI AIALQVPVLA LLILFSHAVS
KALLSMSVGG VIAATNCQDI TELGGLGGRM PATTTAFLVG GAGLVGLVPL GGFLCLAQSV
ELIGARSSGL VVIFLLTNAL TALNLARVYR HVFLGQPLLK TRRAVEVNWQ MAFPMVAMTV
IVILTPIFLI RLESLEGLLA FPLWAAGLVV GSGLIGVVAG TLLPLSKAWS RSINPVVRWL
QDLLAFDFYT ERFYRITIVN VVAGFSRLAY AFDRIVVDGL LHGMARFSLS SAQSLKLSIS
GRSQTYVLTV VAAILLFLSS LSWLLR
//
