UniProtKB - P00393 (NDH_ECOLI)
Type II NADH:quinone oxidoreductase
ndh
Functioni
Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones (PubMed:6784762, PubMed:7009604, PubMed:7020757, PubMed:6362717, PubMed:3122832, PubMed:2679883, PubMed:10664466).
Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient (PubMed:3122832, PubMed:2679883).
7 PublicationsIt may also contribute to copper homeostasis and bacterial oxidative protection (PubMed:7487066, PubMed:10510271, PubMed:16759635, PubMed:21390523).
Shows cupric reductase activity, and catalyzes the reduction of Cu2+ to Cu+ with NADH as electron donor (PubMed:10510271).
Exhibits Cu2+ reductase activity in the presence of either FAD or quinone, but is unable to reduce Fe3+ (PubMed:10510271).
Contains thiolate-bound copper (PubMed:12176061).
5 PublicationsMiscellaneous
Catalytic activityi
Cofactori
Activity regulationi
Kineticsi
- KM=50 µM for NADH (for NADH:quinone oxidoreductase activity)1 Publication
- KM=6.1 µM for NADH (for cupric reductase activity, in the presence of FAD)1 Publication
- KM=6.9 µM for NADH (for cupric reductase activity, in the presence of duroquinone)1 Publication
- KM=34 µM for NADH (for NADH:quinone oxidoreductase activity)1 Publication
- KM=5.9 µM for ubiquinone-11 Publication
- KM=2.3 µM for ubiquinone-21 Publication
- KM=40 µM for ubiquinone-3 (for NADH:quinone oxidoreductase activity)1 Publication
- KM=32 µM for duroquinone (for cupric reductase activity)1 Publication
- KM=18.7 µM for decylbenzoquinone1 Publication
- KM=1.8 µM for idebenone1 Publication
- KM=20 µM for dichlorophenolindophenol1 Publication
- KM=12 µM for decylbenzoquinone (for NADH:quinone oxidoreductase activity)1 Publication
- KM=0.022 nM for Cu2+ (in the presence of FAD)1 Publication
- KM=0.032 nM for Cu2+ (in the presence of duroquinone)1 Publication
- KM=102 µM for FAD (for cupric reductase activity)1 Publication
- Vmax=106 mmol/min/mg enzyme with NADH as substrate1 Publication
- Vmax=106 mmol/min/mg enzyme with ubiquinone-1 as substrate1 Publication
- Vmax=190 mmol/min/mg enzyme with ubiquinone-2 as substrate1 Publication
- Vmax=191 mmol/min/mg enzyme with decylbenzoquinone as substrate1 Publication
- Vmax=107 mmol/min/mg enzyme with idebenone as substrate1 Publication
- Vmax=19.5 mmol/min/mg enzyme with dichlorophenolindophenol as substrate1 Publication
- Vmax=8.8 µmol/min/mg enzyme (for cupric reductase activity, in the presence of FAD)1 Publication
- Vmax=21.1 µmol/min/mg enzyme (for cupric reductase activity, in the presence of duroquinone)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 42 | FAD1 Publication | 1 | |
Binding sitei | 84 | FAD; via amide nitrogen and carbonyl oxygen1 Publication | 1 | |
Binding sitei | 124 | FAD; via amide nitrogen1 Publication | 1 | |
Binding sitei | 275 | NAD; via amide nitrogen1 Publication | 1 | |
Binding sitei | 315 | FAD1 Publication | 1 | |
Binding sitei | 331 | FAD; via amide nitrogen1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 12 – 16 | FAD1 Publication | 5 | |
Nucleotide bindingi | 176 – 181 | NAD1 Publication | 6 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: EcoCyc
- NADH dehydrogenase (ubiquinone) activity Source: EcoCyc
GO - Biological processi
- aerobic electron transport chain Source: EcoCyc
- aerobic respiration Source: EcoCyc
- anaerobic respiration Source: EcoCyc
- copper ion homeostasis Source: EcoCyc
- NADH oxidation Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Electron transport, Transport |
Ligand | FAD, Flavoprotein, NAD, Ubiquinone |
Enzyme and pathway databases
BioCyci | EcoCyc:NADH-DHII-MONOMER |
Protein family/group databases
PeroxiBasei | 5949, EcoNadDH_K12 |
Names & Taxonomyi
Protein namesi | Recommended name: Type II NADH:quinone oxidoreductaseCurated (EC:1.6.5.96 Publications)Alternative name(s): Cupric reductase1 Publication (EC:1.16.1.-1 Publication) NADH dehydrogenase-21 Publication Short name: NADH dh II1 Publication Short name: NDH-21 Publication NADH-quinone reductase1 Publication Short name: NQR1 Publication NADH:ubiquinone oxidoreductase1 Publication Respiratory NADH dehydrogenase1 Publication |
Gene namesi | Name:ndh1 Publication Ordered Locus Names:b1109, JW1095 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell inner membrane 6 Publications; Peripheral membrane protein 1 Publication1 Publication; Cytoplasmic side 1 Publication
Note: Membrane-bound (PubMed:10664466). Interaction with the membrane is probably mediated by amphipathic helices and electrostatic interactions (PubMed:15581635). Copurifies with phospholipids (PubMed:7020757, PubMed:6362717).4 Publications
Plasma Membrane
- plasma membrane Source: EcoCyc
Other locations
- NADH dehydrogenase complex Source: EcoCyc
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000079890 | 2 – 434 | Type II NADH:quinone oxidoreductaseAdd BLAST | 433 |
Proteomic databases
jPOSTi | P00393 |
PaxDbi | P00393 |
PRIDEi | P00393 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Protein-protein interaction databases
BioGRIDi | 4260082, 82 interactors |
DIPi | DIP-10325N |
IntActi | P00393, 9 interactors |
STRINGi | 511145.b1109 |
Family & Domainsi
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1252, Bacteria |
HOGENOMi | CLU_021377_7_0_6 |
InParanoidi | P00393 |
OMAi | DHCIFLD |
PhylomeDBi | P00393 |
Family and domain databases
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR045024, NDH-2 |
PANTHERi | PTHR43706, PTHR43706, 1 hit |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MTTPLKKIVI VGGGAGGLEM ATQLGHKLGR KKKAKITLVD RNHSHLWKPL
60 70 80 90 100
LHEVATGSLD EGVDALSYLA HARNHGFQFQ LGSVIDIDRE AKTITIAELR
110 120 130 140 150
DEKGELLVPE RKIAYDTLVM ALGSTSNDFN TPGVKENCIF LDNPHQARRF
160 170 180 190 200
HQEMLNLFLK YSANLGANGK VNIAIVGGGA TGVELSAELH NAVKQLHSYG
210 220 230 240 250
YKGLTNEALN VTLVEAGERI LPALPPRISA AAHNELTKLG VRVLTQTMVT
260 270 280 290 300
SADEGGLHTK DGEYIEADLM VWAAGIKAPD FLKDIGGLET NRINQLVVEP
310 320 330 340 350
TLQTTRDPDI YAIGDCASCP RPEGGFVPPR AQAAHQMATC AMNNILAQMN
360 370 380 390 400
GKPLKNYQYK DHGSLVSLSN FSTVGSLMGN LTRGSMMIEG RIARFVYISL
410 420 430
YRMHQIALHG YFKTGLMMLV GSINRVIRPR LKLH
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00306 Genomic DNA Translation: CAA23586.1 U00096 Genomic DNA Translation: AAC74193.1 AP009048 Genomic DNA Translation: BAA35924.1 |
PIRi | A00461, DEECR |
RefSeqi | NP_415627.1, NC_000913.3 WP_000211045.1, NZ_STEB01000016.1 |
Genome annotation databases
EnsemblBacteriai | AAC74193; AAC74193; b1109 BAA35924; BAA35924; BAA35924 |
GeneIDi | 66670625 946792 |
KEGGi | ecj:JW1095 eco:b1109 |
PATRICi | fig|1411691.4.peg.1158 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00306 Genomic DNA Translation: CAA23586.1 U00096 Genomic DNA Translation: AAC74193.1 AP009048 Genomic DNA Translation: BAA35924.1 |
PIRi | A00461, DEECR |
RefSeqi | NP_415627.1, NC_000913.3 WP_000211045.1, NZ_STEB01000016.1 |
3D structure databases
AlphaFoldDBi | P00393 |
SMRi | P00393 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4260082, 82 interactors |
DIPi | DIP-10325N |
IntActi | P00393, 9 interactors |
STRINGi | 511145.b1109 |
Protein family/group databases
PeroxiBasei | 5949, EcoNadDH_K12 |
Proteomic databases
jPOSTi | P00393 |
PaxDbi | P00393 |
PRIDEi | P00393 |
Genome annotation databases
EnsemblBacteriai | AAC74193; AAC74193; b1109 BAA35924; BAA35924; BAA35924 |
GeneIDi | 66670625 946792 |
KEGGi | ecj:JW1095 eco:b1109 |
PATRICi | fig|1411691.4.peg.1158 |
Organism-specific databases
EchoBASEi | EB0643 |
Phylogenomic databases
eggNOGi | COG1252, Bacteria |
HOGENOMi | CLU_021377_7_0_6 |
InParanoidi | P00393 |
OMAi | DHCIFLD |
PhylomeDBi | P00393 |
Enzyme and pathway databases
BioCyci | EcoCyc:NADH-DHII-MONOMER |
Miscellaneous databases
PROi | PR:P00393 |
Family and domain databases
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR045024, NDH-2 |
PANTHERi | PTHR43706, PTHR43706, 1 hit |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NDH_ECOLI | |
Accessioni | P00393Primary (citable) accession number: P00393 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families