NUOH_RHOCA
ID NUOH_RHOCA Reviewed; 345 AA.
AC P42032;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 94.
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}; Synonyms=ndhA;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=1568483; DOI=10.1016/0014-5793(92)81250-p;
RA Dupuis A.;
RT "Identification of two genes of Rhodobacter capsulatus coding for proteins
RT homologous to the ND1 and 23 kDa subunits of the mitochondrial Complex I.";
RL FEBS Lett. 301:215-218(1992).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33303 / B10;
RA Dupuis A., Peinnequin A., Darrouzet E., Lunardi J.;
RT "Genetic disruption of the respiratory NADH-ubiquinone reductase of
RT Rhodobacter capsulatus leads to an unexpected photosynthesis-negative
RT phenotype.";
RL FEMS Microbiol. Lett. 148:107-114(1997).
RN [3]
RP SUBCELLULAR LOCATION IN CHROMATOPHORE.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9632256; DOI=10.1046/j.1365-2958.1998.00814.x;
RA Dupuis A., Darrouzet E., Duborjal H., Pierrard B., Chevallet M.,
RA van Belzen R., Albracht S.P.J., Lunardi J.;
RT "Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the
RT mitochondrial ND subunits are all essential for the biogenesis of the
RT respiratory NADH-ubiquinone oxidoreductase.";
RL Mol. Microbiol. 28:531-541(1998).
RN [4]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 11166 / DSM 1710 / CCUG 31484 / JCM 21090 / LMG 2962 / NBRC
RC 16435 / NCIMB 8254 / ATH 2.3.1;
RX PubMed=11245799; DOI=10.1016/s0005-2728(00)00265-6;
RA Roth R., Haegerhaell C.;
RT "Transmembrane orientation and topology of the NADH:quinone oxidoreductase
RT putative quinone binding subunit NuoH.";
RL Biochim. Biophys. Acta 1504:352-362(2001).
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 -!- 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 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex (Probable).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|PubMed:11245799, ECO:0000269|PubMed:9632256}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01350,
CC ECO:0000269|PubMed:11245799, ECO:0000269|PubMed:9632256}.
CC -!- DISRUPTION PHENOTYPE: No functional NADH-quinone oxidoreductase
CC complex. Cells lacking this gene have a nearly normal respiratory
CC growth phenotype on lactate, however they are unable to perform
CC anaerobic photosynthesis. It is suggested that in R.capsulatus this
CC complex may function in reverse flow under physiological conditions.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF029365; AAC24997.1; -; Genomic_DNA.
DR PIR; S22368; S22368.
DR AlphaFoldDB; P42032; -.
DR SMR; P42032; -.
DR GeneID; 31490409; -.
DR OMA; WSGWASN; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
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 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; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 1: Evidence at protein level;
KW Membrane; NAD; Quinone; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..345
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000117531"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 16..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 87..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 107..110
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 111..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 131..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 157..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 177..191
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 192..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 212..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 246..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 266..276
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 277..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 297..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11245799"
FT TRANSMEM 314..333
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TOPO_DOM 334..345
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:11245799"
SQ SEQUENCE 345 AA; 37852 MW; 5F9E9D640D911854 CRC64;
MADFWATSLG QTLILLAQGL GIIAFVMIGL LLLVWGDRKI WAAVQMRKGP NVVGAFGLLQ
SVADAAKYVF KEIVVPAGVD KPVYFLAPML SLVLALLAWV VVPFNEGWVM ADINVAVLFV
FAVSSLEVYG VIMGGWASNS KYPFLGSLRS AAQMISYEVS MGLIIVGVII STGSMNLSAI
VEAQRGDFGL LNWYWLPHLP MVALFFISAL AETNRPPFDL PEAESELVAG FMVEYSSTPY
LLFMAGEYIA VWLMCALTSV LFFGGWLSPI PGVPDGVLWM VAKMAAVFFV FAMVKAIVPR
YRYDQLMRIG WKVFLPLSLA WVVVVAFLAK FEVLGGFWAR WSIGA
