ID A0A1I6JVH4_9SPHN Unreviewed; 483 AA.
AC A0A1I6JVH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN05192580_0934 {ECO:0000313|EMBL:SFR82888.1};
OS Sphingomonas jatrophae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166337 {ECO:0000313|EMBL:SFR82888.1, ECO:0000313|Proteomes:UP000198824};
RN [1] {ECO:0000313|EMBL:SFR82888.1, ECO:0000313|Proteomes:UP000198824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5-249 {ECO:0000313|EMBL:SFR82888.1,
RC ECO:0000313|Proteomes:UP000198824};
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|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; FOZG01000001; SFR82888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6JVH4; -.
DR STRING; 1166337.SAMN05192580_0934; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000198824; 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.
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 Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000198824};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 160..184
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 204..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 298..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 321..344
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 370..391
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 125..419
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 483 AA; 50412 MW; A457D88136562DAF CRC64;
MGAALLLTLP ELILSLTSLA LLMVAAYAGD RSVRMVSILS VAALVAAAFA ALLPPTGYGI
AFGGLYRADA FSAFAKLLIY VAAGVSIVIA PAFFHRAPGQ GGTLRAEYPI LILLSTIGTG
MMVSAGDMLT LYVGLELQSL ASYVLASFMR RDLRSAESGL KYFVLGALAS GILLYGISLV
YGFTGTTQYD GIAVAFREGL STGQLFGLVF VFAGLAFKIA AVPFHMWTPD VYEGAPTPVT
AFFATAQKVG AVALLLRVAV EAMGSASDAW MQIVIFSALA STILGGVAAI GQSNIKRLLA
YSSINNVGFA LFGLVPGDAN GVSSVLTYLA VYIVMTLGSF LCILRMRDAE GRPVEEISAL
SGLSRLRPGL AAALAIFMFS LAGIPPLFGF WPKFLVFDAL VAIGMWPLAM VGIATSVIGA
YYYLKIVKTM YFDEPATPFG ASPDRVEGGL IAVGALIVSP LGYLLIGPLG AYSLAAARAL
FPG
//
