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Database: UniProt
Entry: A0A1S6IXA9_9FIRM
LinkDB: A0A1S6IXA9_9FIRM
Original site: A0A1S6IXA9_9FIRM 
ID   A0A1S6IXA9_9FIRM        Unreviewed;       644 AA.
AC   A0A1S6IXA9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:AQS59413.1};
GN   ORFNames=B0537_10135 {ECO:0000313|EMBL:AQS59413.1};
OS   Desulforamulus ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS59413.1, ECO:0000313|Proteomes:UP000189464};
RN   [1] {ECO:0000313|EMBL:AQS59413.1, ECO:0000313|Proteomes:UP000189464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSS09 {ECO:0000313|EMBL:AQS59413.1,
RC   ECO:0000313|Proteomes:UP000189464};
RX   PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA   Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT   "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT   sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT   compost.";
RL   Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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 CPA3 antiporters (TC 2.A.63) subunit A
CC       family. {ECO:0000256|ARBA:ARBA00008483}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC       {ECO:0000256|ARBA:ARBA00008200}.
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DR   EMBL; CP019698; AQS59413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6IXA9; -.
DR   STRING; 1833852.B0537_10135; -.
DR   KEGG; dfg:B0537_10135; -.
DR   OrthoDB; 9807568at2; -.
DR   Proteomes; UP000189464; Chromosome.
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:UP000189464};
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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        425..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        508..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..123
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          139..417
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          444..581
FT                   /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT                   chloroplast chain 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01010"
SQ   SEQUENCE   644 AA;  70697 MW;  F487A1AD5E1A4570 CRC64;
     MVDFALTHAW LVPLLPALAF VIIVFLTRPY ARLSSTVAIA AIFSSFVLAA NIAYGVFTNP
     GFIEKPLVYS LRWFGMEGFT VDVGVMLDPT SAMMLFMVSM VATLIQIYST GYMHGDPQYS
     VFFSYLSLFA ASMLGLVISS NLLQMFILWE LVGLCSFLLI GFYTFKVSAR EAAKKAFITT
     RIGDFGMMLG LLFLQIVFGT LDLVGLAERV PNYEQFGISL GLLTLIAILL FIGPIGKSGQ
     FPLHVWLPDA MEGPTPVSAL IHAATMVVAG VYLVGRTLFL FAEVPGAAEV VAFIGAFTAI
     FAATIAITQR EIKRILAYST VSQLGYMMLA LGVGSLSASM FHLWTHAFFK ALMFLGAGSV
     LHALHDKADV WEMGGLIKKM PITGWTFVIG GLAIAGIPPF AGFWSKDEIL LVTLEYAKHG
     HALGYLLFFF AAVTAFLTAF YMWRLIFLTF FGKEKPENHP HESPLSMTFP LVVLAVLAAV
     GGLVGTPWAN VWGEWIHFGD VHHGDPNYAL MILSVVLAVA GIGLAYRLYY QDEEKQLAKQ
     LAERYQSLYK LSYNKYYVDE LYAWFTRTVV DAGAKALYWF DIYVVDNIVN GLAGVTKLSG
     QGMRFLHTGK MQTYALVFFL ALLVITVVLA YGNPTLAGSL GGVN
//
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