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Database: UniProt
Entry: A0A1M6XPW8_9RHOB
LinkDB: A0A1M6XPW8_9RHOB
Original site: A0A1M6XPW8_9RHOB 
ID   A0A1M6XPW8_9RHOB        Unreviewed;       704 AA.
AC   A0A1M6XPW8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:SHL07953.1};
GN   ORFNames=SAMN05444398_101514 {ECO:0000313|EMBL:SHL07953.1};
OS   Roseovarius pacificus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=337701 {ECO:0000313|EMBL:SHL07953.1, ECO:0000313|Proteomes:UP000183974};
RN   [1] {ECO:0000313|EMBL:SHL07953.1, ECO:0000313|Proteomes:UP000183974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29589 {ECO:0000313|EMBL:SHL07953.1,
RC   ECO:0000313|Proteomes:UP000183974};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
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}.
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DR   EMBL; FRBR01000001; SHL07953.1; -; Genomic_DNA.
DR   RefSeq; WP_073032334.1; NZ_FRBR01000001.1.
DR   AlphaFoldDB; A0A1M6XPW8; -.
DR   STRING; 337701.SAMN05444398_101514; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000183974; 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   Reference proteome {ECO:0000313|Proteomes:UP000183974};
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..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        383..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        679..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..109
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          135..440
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   704 AA;  77571 MW;  CDDBC42DA3CECE6B CRC64;
     MELTILFAPL IGAIIAGFGW RIIGETGAQW LTTGLLFLSC ILSWIVFLGH DGQTHIVHIL
     DWIESGTLST SWAIRLDRLT AIMLIVVTSV SALVHLYSMG YMAHDENFRE GESYKPRFFA
     YLSLFTFAML MLVTADNLAQ MFFGWEGVGL ASYLLIGFYF RKPSANAASI KAFVVNRVGD
     FGFILGIMAL YFLTDSIRFE DIFAAGPELA ETQLSFLWTE WNAANLIAFL LFVGAMGKSA
     QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP IMEYAPEAMG FVTFIGATTA
     FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGVGVYSVA MFHLFTHAFF KAMLFLGAGS
     VIHGMHHEQD MRNYGGLRKK LPYTFWAMLI GTLAITGVGI PLTHFGFAGF LSKDAVIESA
     YAGTAGGYAF WMLVIAALFT SFYSWRLMFL TFWGKPRGDK HTHDHAHESP TVMLVPLGVL
     ALGAVFSGMV WYNSFFGDHA QVNKFFGIPV HHAEADAGHG EETATEDQAA ADASNDEAAV
     QEGGEPAAAI HAMAPEGAIF MGPDNHVMDD AHHAPTWVKI SPFIAMVIGF VVALWFYIWD
     PSMPRKLAEN QRPLYQFLLN KWYFDEIYDF LFVRPTKALG RFLWKRGDGD VVDGTINGVA
     MGIIPFFTRL AGRAQSGYIF TYAFAMVIGI AVLVTWMTFI GGAE
//
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