ID A0A1B6YCV2_9BACT Unreviewed; 673 AA.
AC A0A1B6YCV2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:OAN63780.1};
GN ORFNames=A8B79_14540 {ECO:0000313|EMBL:OAN63780.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN63780.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN63780.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN63780.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001558};
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:OAN63780.1}.
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DR EMBL; LXYG01000005; OAN63780.1; -; Genomic_DNA.
DR RefSeq; WP_066217795.1; NZ_LXYG01000005.1.
DR AlphaFoldDB; A0A1B6YCV2; -.
DR STRING; 1849360.A8B79_14540; -.
DR InParanoid; A0A1B6YCV2; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000078514; 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:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_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; PF01010; Proton_antipo_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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000078514};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..125
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 142..429
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 480..582
FT /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT chloroplast chain 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01010"
SQ SEQUENCE 673 AA; 74425 MW; C3267F48FEFF69B3 CRC64;
MESATALFSL IIALPLLGFL INGLTGLFVE SYRNKKQLIG SIASTAVFIP FVIAVYFFIN
MNAGSEALIY KLFTWMDVGT FSVDVAYRVD QLSVMMTMVV TGVGFLIHIY SMGYMSHDEG
YWKFFAYLNL FIFAMLNLVL GNNLLLLFLG WEGVGVCSYL LIGFWYTDMA KSDAAKKAFI
YNRIGDFAFL IAMFMVFQTV GSLNFDVILG NLDSFTEGYM VAIGLLMFVG ATGKSAQIPL
FVWLPDAMAG PTPVSALIHA ATMVTSGIYL ISRMSPMYAM IPEVMIIISV IGALTAIVAA
TIAITQNDIK GVLAYSTVSQ LGYMFLALGA GGFTAAMFHV VTHAFFKACL FLGSGSVIHA
MEHVEHGLHK EGKDVHFDPQ DMRFMGGLKK YMPSTYKTFL IATVAIAGIP PLAGFFSKDE
VLAMTMNAGF VDGGSWVYMM LWGVGIITAF LTAFYMFRLT LTTFHGSFKL PTKIKEAAGS
EKFLHENPWN MTTPLWILAV LAVFGGFLGV PNFIVETFTH EPAHINLLHD WLYKINADYI
IEMEHWVEWV LMAVSILIAI SGVWLAFRMY NNDQQEESDA KIASRFGGLY SVWKDKYNLD
DVYEGLVANP TVKFSDKVLA VFDMKVVDGI VNAIAGTVRL FGSLFRYLQT GVVSSYALAF
VIGVIVILYL MIS
//