ID A0A2M9R6J9_9FLAO Unreviewed; 627 AA.
AC A0A2M9R6J9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:PJR04333.1};
GN ORFNames=CDL10_07135 {ECO:0000313|EMBL:PJR04333.1};
OS Avrilella dinanensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Avrilella.
OX NCBI_TaxID=2008672 {ECO:0000313|EMBL:PJR04333.1, ECO:0000313|Proteomes:UP000231960};
RN [1] {ECO:0000313|EMBL:PJR04333.1, ECO:0000313|Proteomes:UP000231960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UR159 {ECO:0000313|EMBL:PJR04333.1,
RC ECO:0000313|Proteomes:UP000231960};
RA Leyer C., Sassi M., Minet J., Kayal S., Cattoir V.;
RT "Description of Avrilella dinanensis gen. nov. sp. nov.";
RL Submitted (JUN-2017) 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 -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC {ECO:0000256|ARBA:ARBA00008200}.
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:PJR04333.1}.
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DR EMBL; NIPO01000001; PJR04333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9R6J9; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000231960; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000231960};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
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..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..117
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 134..424
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 438..560
FT /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT chloroplast chain 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01010"
SQ SEQUENCE 627 AA; 68526 MW; 3F95AC81FBE1F7A0 CRC64;
MELSILITII LPLVGFLLLF LGGRSISNKL SGAIATLTVA ASFVLSILIF TSIKSTGESI
HIHLFDWIQF ADFKIDFAFH IDQLNALWLL FVTGIGALIH WYSTSYMKGD DDYNKYFSYL
NLFVFFMLVL VSGSNLLIMF IGWEGVGLCS YLLIGFWHKN QAFNDAAKKA FIMNRIGDLG
FLIGAFILIS LYNTIDFVEL RQLTEHGTSL AALPLLGGAT LALFVAAAGK SAQIPLYTWL
PDAMAGPTPV SALIHAATMV TAGIFMITRL NFIFDLTPDV QNIIAVVGAL TSLLAASIGL
AQNDIKKVLA YSTVSQLGLM FLAIGLGAYE IAVFHVITHA FFKACLFLGS GSVIHAVGGE
QDMRHMGGLK KYMGITYVTF LISSLAISGI PPFSGFFSKD EILMTAFHNN MVLYIIGSLA
SIMTAFYMFR LIYLTFFNQF RGTEEQKSHL HESPKSMTTP LIVLAILATV GGAISLPGSS
WLNDFLAPAI VHNAAAHPHE LGTTEYLLMA VAVVGALIGI GLAYNKYGKG KFVPGNDNQL
SGIQKVLSNK FYIDEIYNVL IVSPINWLGS VFKTIFEPLI AGIVLSFGRF AHELSYQGKK
AQNGNIGLYL FAFVFGICAI VYYLFIR
//
