NUOH_PSEAE
ID NUOH_PSEAE Reviewed; 331 AA.
AC Q9I0J5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NADH dehydrogenase I subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
GN Name=nuoH {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=PA2643;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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. This subunit may bind ubiquinone.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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_01350};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR EMBL; AE004091; AAG06031.1; -; Genomic_DNA.
DR PIR; H83314; H83314.
DR RefSeq; NP_251333.1; NC_002516.2.
DR RefSeq; WP_003090465.1; NZ_QZGE01000008.1.
DR AlphaFoldDB; Q9I0J5; -.
DR SMR; Q9I0J5; -.
DR STRING; 287.DR97_5319; -.
DR PaxDb; Q9I0J5; -.
DR PRIDE; Q9I0J5; -.
DR DNASU; 882350; -.
DR EnsemblBacteria; AAG06031; AAG06031; PA2643.
DR GeneID; 882350; -.
DR KEGG; pae:PA2643; -.
DR PATRIC; fig|208964.12.peg.2766; -.
DR PseudoCAP; PA2643; -.
DR HOGENOM; CLU_015134_0_1_6; -.
DR InParanoid; Q9I0J5; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; Q9I0J5; -.
DR BioCyc; PAER208964:G1FZ6-2683-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..331
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000244930"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 331 AA; 36744 MW; D73C0565DB16EAD7 CRC64;
MSWLTPALVT IILTVVKAIV VLLAVVICGA LLSWVERRLL GLWQDRYGPN RVGPFGAFQL
GADMVKMFFK EDWTPPFADK MIFTLAPVIA MGALLVAFAI VPITPTWGVA DLNIGILFFF
AMAGLTVYAV LFAGWSSNNK FALLGSLRAS AQTISYEVFL ALSLMGIVAQ VGSFNMRDIV
QYQIDNVWFI IPQFFGFCTF IIAGVAVTHR HPFDQPEAEQ ELADGYHIEY AGMKWGMFFV
GEYIGIVLVS ALLATLFFGG WHGPFLDTLP WLSFFYFAAK TGFFIMLFIL IRASLPRPRY
DQVMAFSWKV CLPLTLINLL VTGALVLAAA Q
