ID A0A073JJS3_9RHOB Unreviewed; 706 AA.
AC A0A073JJS3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=NADH:ubiquinone oxidoreductase subunit L {ECO:0000313|EMBL:KEJ97972.1};
GN ORFNames=SUH3_03000 {ECO:0000313|EMBL:KEJ97972.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ97972.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ97972.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ97972.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) 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}.
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:KEJ97972.1}.
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DR EMBL; JAMD01000001; KEJ97972.1; -; Genomic_DNA.
DR RefSeq; WP_037921252.1; NZ_WKFG01000017.1.
DR AlphaFoldDB; A0A073JJS3; -.
DR GeneID; 68870522; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000027746; 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:UP000027746};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubiquinone {ECO:0000313|EMBL:KEJ97972.1}.
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..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..702
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"
FT REGION 523..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 77105 MW; B8C6299CF6587132 CRC64;
MELTILFAPL VGAILCGFGW RAFGETAAMC IATGLLFLSA LLSWVVFLSF DGTTETIQIL
RWIESGSLST DWAIRLDRLT AIMLIVITTV SSLVHLYSFG YMDHDPQWKD DESYKPRFFA
YLSFFTFAML MLVTSDNLVQ MFFGWEGVGV ASYLLIGFYY RKPSANAAAI KAFVVNRVGD
FGFSLGIFAL FFLTDSIRFD DIFAAAPGLA ETQLSFLWGE WNAANLIAIL LFIGAMGKSA
QLLLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLICRMSP IMEFAPEATM FITFIGATTA
FFAATVGLVQ TDIKRVIAYS TCSQLGYMFV AAGVGMYSAA MFHLLTHAFF KAMLFLGAGS
VIHAMHHEQD MTNYGGLRKK IPYTFAAMMI GTLAITGVGI PLTHIGFAGF LSKDAIIESA
YGGGSMYGFW MLVIAAAFTS FYSWRLIFLT FYGEPRGDKH THDHAHESPM VMLIPLGVLS
LGAIFAGMIW YNSFFGHADQ VGKFYGIPVA EAGADGAAHV EGAAESHGEA AATEEHATAE
GGHGAAGEHH LAFAGKPGEG ALYMGPDNHV LEDAHATPVW VKVSPFIAML AGFLMALWFY
IWNPTLPARL AENQRPIYLF LKNKWYFDEL YDVVFVRPAK WIGRQLWKKG DGNVIDGTLN
GVALGIVPFL TRLAGRAQSG YIFTYAFAMV IGIAVLITWM TLGGAN
//
