ID A0A1H7GFZ4_9RHOB Unreviewed; 686 AA.
AC A0A1H7GFZ4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:SEK36984.1};
GN ORFNames=SAMN05443999_101297 {ECO:0000313|EMBL:SEK36984.1};
OS Roseovarius azorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1287727 {ECO:0000313|EMBL:SEK36984.1, ECO:0000313|Proteomes:UP000199582};
RN [1] {ECO:0000313|EMBL:SEK36984.1, ECO:0000313|Proteomes:UP000199582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100674 {ECO:0000313|EMBL:SEK36984.1,
RC ECO:0000313|Proteomes:UP000199582};
RA de Groot N.N.;
RL Submitted (OCT-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; FOAG01000001; SEK36984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7GFZ4; -.
DR STRING; 1287727.SAMN05443999_101297; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000199582; 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:UP000199582};
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..194
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..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..681
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 686 AA; 75710 MW; BD0375880B47961E CRC64;
METILLFAPL VGAIIAGFGW RVIGDAGAQW LATGLLFLSC LLSWIVFLAH DGITQQVHIL
DWVQSGTLDT AWAIRMDRLT AIMLIVITTV SALVHLYSVG YMAHDENFRE NESYRPRFFA
YLSFFTFAML MLVTSDNLLQ MFFGWEGVGV ASYLLIGFYY RKPSANAAAI KAFVVNRVGD
FGFALAIMAL YFLVDSIRLD DIFAAAPQLA ETQVTFLWTE WNAANLIAFL LFVGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LMEYAPEALN FVVFIGASTA
FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGVGVYSVA MFHLFTHAFF KAMLFLGAGS
VIHGMHHEQD MRNYGGLRKK MPYTFWAMMI GTLAITGVGI PLTHIGFAGF LSKDAVIESA
WAGTAGGYGF WMLVIAALFT SFYSWRLMFM TFYGESRGDR HTHEHAHESP MVMLVPLGAL
ALGAVFAGMV WFNSFFGSHD QVNSFFGIPV HHVEASEGHA DEGEAAEEHG PAHAGAPQGA
IFMHPDNHVM DEAHHAPTWV KVSPFVAMLI GFVTAFWFYI LDPSMPRKVA ETNRPLYLFL
LNKWYFDEIF DWLLVRPAKA LGQILWKRGD GDVIDGSLNG VAMGLIPRLT RLAGRAQSGY
IFTYAFAMVI GIAILVTWMT IFGGGN
//
