ID C7D818_9RHOB Unreviewed; 698 AA.
AC C7D818;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=NADH-quinone oxidoreductase subunit l {ECO:0000313|EMBL:EET47659.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:EET47659.1};
GN ORFNames=TR2A62_1164 {ECO:0000313|EMBL:EET47659.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET47659.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET47659.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET47659.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) 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; GG697169; EET47659.1; -; Genomic_DNA.
DR RefSeq; WP_009158730.1; NZ_GG697169.2.
DR AlphaFoldDB; C7D818; -.
DR STRING; 633131.TR2A62_1164; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_5; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000004701; 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:EET47659.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004701};
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 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..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..108
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 135..439
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 698 AA; 77016 MW; B2E96F76FAD7C9BB CRC64;
MEKIILFAPL IGSLLCGFGW KFIGQTAAQW VSTSLLFLAA FLSWVVFLSH NGTTEYIHVL
DFIQSGTLDT SWAIRMDRLT AIMLIVITTV SALVHLYSFG YMAHDENFKE GEVYRPRFFA
YLSFFTFSML MLVTSDNLVQ MFFGWEGVGV ASYLLIGFYY RKPTANAAAI KAFVVNRVGD
FGFALGIFGL YFLADSIKFD DVFAAVPTIA ETQLTFLWRD WNAAELIAIL LFIGAMGKSA
QLILHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LMEFAPMATN FIVFLGATTA
FFAATVGLVQ NDIKRVIAYS TCSQLGYMFV AAGVGVYSVA MFHLFTHAFF KAMLFLGAGS
VIHGMHHEQD MRNYGGLRKK LPYTFWAMMI GTLAITGVGI PLTHIGFAGF LSKDAVIESA
FAGGTSYAFW LLVIAAFMTS FYSWRLMFLT FFGTPRGDKH THEHAHEGPM TMLVPLGVLS
LGAIFAGMIW YDDFFGKEND VAAFFGTHQI EEHAAAAGAG FSLIAPAYAA TEENDDHGKD
EKLAKQVIGD GAIYMGPENH VLHDAHYVPK WVKVSPFIAM ISGLALAFWF YIVNPSLPGR
LAANQRPLYL FFLNKWYFDE IYDFVFVKPA MALGRLLWKR GDGNIIDGSI NGVALGIVPF
LTRLVGRGQS GYLFHYAFAM VLGIAILLTW MMLGGGAG
//
