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Database: UniProt
Entry: A0A0F7KR66_9SPHN
LinkDB: A0A0F7KR66_9SPHN
Original site: A0A0F7KR66_9SPHN 
ID   A0A0F7KR66_9SPHN        Unreviewed;       487 AA.
AC   A0A0F7KR66;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH dehydrogenase I subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NDH-1 subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
GN   Name=nuoN {ECO:0000256|HAMAP-Rule:MF_00445,
GN   ECO:0000313|EMBL:AKH41677.1};
GN   ORFNames=FHS61_002167 {ECO:0000313|EMBL:MBB5733141.1}, WYH_00621
GN   {ECO:0000313|EMBL:AKH41677.1};
OS   Croceibacterium atlanticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH41677.1, ECO:0000313|Proteomes:UP000034392};
RN   [1] {ECO:0000313|EMBL:AKH41677.1, ECO:0000313|Proteomes:UP000034392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26DY36 {ECO:0000313|EMBL:AKH41677.1,
RC   ECO:0000313|Proteomes:UP000034392};
RA   Wu Y.-H., Cheng H., Wu X.-W.;
RT   "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5733141.1, ECO:0000313|Proteomes:UP000556014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5733141.1,
RC   ECO:0000313|Proteomes:UP000556014};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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|HAMAP-Rule:MF_00445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00445};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00445}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|HAMAP-Rule:MF_00445}.
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DR   EMBL; CP011452; AKH41677.1; -; Genomic_DNA.
DR   EMBL; JACIJL010000004; MBB5733141.1; -; Genomic_DNA.
DR   RefSeq; WP_046902664.1; NZ_JACIJL010000004.1.
DR   AlphaFoldDB; A0A0F7KR66; -.
DR   STRING; 1267766.WYH_00621; -.
DR   KEGG; aay:WYH_00621; -.
DR   PATRIC; fig|1267766.3.peg.627; -.
DR   OrthoDB; 9811718at2; -.
DR   Proteomes; UP000034392; Chromosome.
DR   Proteomes; UP000556014; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   NCBIfam; TIGR01770; NDH_I_N; 1.
DR   PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Oxidoreductase {ECO:0000313|EMBL:AKH41677.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034392};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00445};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00445}; Transport {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00445}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        109..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        134..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        165..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        207..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        242..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        301..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        372..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        406..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   DOMAIN          128..422
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   487 AA;  50585 MW;  C36D428938F7B8B5 CRC64;
     MEFKASLALI APEILLSLSG LALLLVAAWS GDKASRTISV LACVALGACF FLVAPAVCAG
     AAGPDTMAFG GQFRADAFAG FAKLMIFAAS GAVLIVAPSF LERTGSMRAE FPVLVLFATL
     GMSIMVSATD LLTLYIGLEL NSLSAYVLAA FLRSDNRSAE AGLKYFVLGA LASGILLFGM
     SLTYGFTGTT SFEGIRVALD GELATGALFG LIFVLAGLAF KMSAVPFHMW TPDVYEGAPT
     PVTAFFATAP KVAAVALTAR VALDPFGMQA DAWQQIVVFA ALASIVVGAL GAIGQSNVKR
     LLAYSSINNI GFILIGLATG TLAGASAMLV YLAIYVAMTV GSFVAVLMLR DADGNPVEAI
     SDLAGLSTTR PALAWCLMAL MFSTAGIPPL FGFWGKFVVF RAAVEADLIV LAALGIAASV
     IGAFYYIKIV KIMFFDEPAN KVVGKSDWSH WALLAISTVF ISPLGYLLTG WLGDLADSAA
     ASLLLLA
//
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