NUON_ANAMF
ID NUON_ANAMF Reviewed; 481 AA.
AC B9KIT6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=AMF_549;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(2009).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; CP001079; ACM49398.1; -; Genomic_DNA.
DR RefSeq; WP_010267787.1; NC_012026.1.
DR AlphaFoldDB; B9KIT6; -.
DR SMR; B9KIT6; -.
DR STRING; 320483.AMF_549; -.
DR EnsemblBacteria; ACM49398; ACM49398; AMF_549.
DR GeneID; 7398164; -.
DR KEGG; amf:AMF_549; -.
DR PATRIC; fig|320483.3.peg.642; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_5; -.
DR OMA; NAWAPDA; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000007307; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Pfam; PF00361; Proton_antipo_M; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..481
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391095"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 481 AA; 52585 MW; 600664ED43109EA3 CRC64;
MCWRELLYML PELYLLGSAM IALLLGIVVD ARWVHRLSAV SMGVVVVLSW WSGVTDHVAE
DVHLFNGLVL HTRYTCISRM LVGVAGFVAS LLFLCARREV RYEFSVVMLF ATLGAMTLVQ
AGHFLSLYIS LELNSLSSCV LVCFNRSSER ASESALKFFI LSALSSCIML YGISLVYGYS
TGLECNVMQE ILAGRASLGA TLGCAFVLVG VLFKLAVVPF HMWAVDTYHG SPMAAMAFFL
IVTKSAAILL LARIVGENGI LQQSILYGII SVSGLSALVG ELGALRQSNI KRLLAYSNIG
QLGYVLPVVV LHGTSSYAIF HYVLTSWVIN AWIFSVLLRY DDEGFELASL AGMHRSSPFV
AFALVVSMVS AAGFPPFLGC WPKYFFLKSI VMSDIPTVVA FPYVLLVCAV GIVPCFYCFR
IARVVYFDQP AMGAGHPALP HHLGLTVIAV VCMLLSVIAL FLAQYFDILF QGLVWVFGGR
T
