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Database: UniProt
Entry: H0THI8_9BRAD
LinkDB: H0THI8_9BRAD
Original site: H0THI8_9BRAD 
ID   H0THI8_9BRAD            Unreviewed;       704 AA.
AC   H0THI8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=NADH-quinone oxidoreductase chain L (NADH dehydrogenase I, chain L) (NDH-1, chain L) {ECO:0000313|EMBL:CCE05926.1};
DE            EC=1.6.5.3 {ECO:0000313|EMBL:CCE05926.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:CCE05926.1};
GN   Name=nuoL {ECO:0000313|EMBL:CCE05926.1};
GN   ORFNames=BRAS3843_1500032 {ECO:0000313|EMBL:CCE05926.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE05926.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCE05926.1}.
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DR   EMBL; CAFK01000058; CCE05926.1; -; Genomic_DNA.
DR   RefSeq; WP_008968449.1; NZ_CAFK01000058.1.
DR   AlphaFoldDB; H0THI8; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000002686; 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; 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; 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   Oxidoreductase {ECO:0000313|EMBL:CCE05926.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686};
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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        136..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        576..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        679..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..176
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          192..486
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   704 AA;  77414 MW;  27B4CFE008DEC183 CRC64;
     MIQAIVFLPL LGAILAGLIA LFGAHARNPS GDTVEHHDDG HHHGTAAHVG GDAALVHVAH
     DEPLAHDDHG HGHDDHHVAE PPAAGSRGAE LITTALLFVA AALSWATLIN VGFLHHDAGV
     LELFPWINSG ELQVSWALRV DTLTAVMLVV VTTVSSLVHL YSIGYMDEDP NRPRFFGYLS
     LFTFAMLMLV TANNLVQLFF GWEGVGLASY LLIGFWYQRP SANAAAIKAF VVNRVGDFGF
     ALGIFAVFWL TNSTDFETIF HAAPSLTGKT INLLGWHADA LTLTCLLLFM GAMGKSAQFL
     LHTWLPDAME GPTPVSALIH AATMVTAGVF MVARLSPLFE LAPNAQAVVM FVGATTAFFA
     ATVGLVQNDI KRIVAYSTCS QLGYMFVAMG AGAYSVGMFH LFTHAFFKAL LFLGSGSVIY
     AMHHEQDIRN MGGLWRKIPY TFAVMCVGTM ALTGVPGFAG FFSKDAIIES AYASHNTFAT
     YAYFLTVVAA GLTSFYSWRL IWKTFFGTPH DQHHYEAAHE SPIWMLIPIG VLAAGSILAG
     FPFKELFVGE HGVEEFFRES VKMNPHILAD MEHMPFWLGQ LPLFMMIGGF AISYFFYISR
     PDIPEELASQ QPLLYNFLLN KWYFDELYDV IFVRPAKWLG RFLWKKGDGF VIDGFGPDGV
     SARVLDITRN VVKIQTGYLY HYAFAMLIGV AGLITWFMFM GGQQ
//
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