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Protein

NADH-quinone oxidoreductase subunit L

Gene

nuoL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Catalytic activityi

NADH + a quinone = NAD+ + a quinol.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled electron transport Source: InterPro
  • electron transport coupled proton transport Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
LigandNAD, Ubiquinone

Enzyme and pathway databases

BioCyciEcoCyc:NUOL-MONOMER
MetaCyc:NUOL-MONOMER

Protein family/group databases

TCDBi3.D.1.1.1 the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit L (EC:1.6.5.11)
Alternative name(s):
NADH dehydrogenase I subunit L
NDH-1 subunit L
NUO12
Gene namesi
Name:nuoL
Ordered Locus Names:b2278, JW2273
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12092 nuoL

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6PeriplasmicSequence analysis6
Transmembranei7 – 23HelicalSequence analysisAdd BLAST17
Topological domaini24 – 31CytoplasmicSequence analysis8
Transmembranei32 – 52HelicalSequence analysisAdd BLAST21
Topological domaini53 – 74PeriplasmicSequence analysisAdd BLAST22
Transmembranei75 – 99HelicalSequence analysisAdd BLAST25
Topological domaini100 – 115CytoplasmicSequence analysisAdd BLAST16
Transmembranei116 – 133HelicalSequence analysisAdd BLAST18
Topological domaini134 – 210PeriplasmicSequence analysisAdd BLAST77
Transmembranei211 – 228HelicalSequence analysisAdd BLAST18
Topological domaini229 – 248CytoplasmicSequence analysisAdd BLAST20
Transmembranei249 – 267HelicalSequence analysisAdd BLAST19
Topological domaini268 – 281PeriplasmicSequence analysisAdd BLAST14
Transmembranei282 – 300HelicalSequence analysisAdd BLAST19
Topological domaini301 – 306CytoplasmicSequence analysis6
Transmembranei307 – 325HelicalSequence analysisAdd BLAST19
Topological domaini326 – 338PeriplasmicSequence analysisAdd BLAST13
Transmembranei339 – 356HelicalSequence analysisAdd BLAST18
Topological domaini357 – 373CytoplasmicSequence analysisAdd BLAST17
Transmembranei374 – 397HelicalSequence analysisAdd BLAST24
Topological domaini398 – 413PeriplasmicSequence analysisAdd BLAST16
Transmembranei414 – 437HelicalSequence analysisAdd BLAST24
Topological domaini438 – 454CytoplasmicSequence analysisAdd BLAST17
Transmembranei455 – 472HelicalSequence analysisAdd BLAST18
Topological domaini473 – 494PeriplasmicSequence analysisAdd BLAST22
Transmembranei495 – 514HelicalSequence analysisAdd BLAST20
Topological domaini515 – 589CytoplasmicSequence analysisAdd BLAST75
Transmembranei590 – 607HelicalSequence analysisAdd BLAST18
Topological domaini608 – 613PeriplasmicSequence analysis6

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001182131 – 613NADH-quinone oxidoreductase subunit LAdd BLAST613

Keywords - PTMi

Quinone

Proteomic databases

PaxDbiP33607
PRIDEiP33607

Interactioni

Subunit structurei

Composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

Protein-protein interaction databases

BioGridi4260888, 94 interactors
ComplexPortaliCPX-243 Respiratory chain complex I
DIPiDIP-10388N
IntActiP33607, 1 interactor
STRINGi316385.ECDH10B_2440

Structurei

3D structure databases

ProteinModelPortaliP33607
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I subunit 5 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D65 Bacteria
COG1009 LUCA
HOGENOMiHOG000100570
InParanoidiP33607
KOiK00341
OMAiQFYALIV
PhylomeDBiP33607

Family and domain databases

InterProiView protein in InterPro
IPR003945 NADHpl_OxRdtase_5
IPR018393 NADHpl_OxRdtase_5_subgr
IPR001750 ND/Mrp_mem
IPR001516 Proton_antipo_N
PfamiView protein in Pfam
PF00361 Proton_antipo_M, 1 hit
PF00662 Proton_antipo_N, 1 hit
PRINTSiPR01435 NPOXDRDTASE5
TIGRFAMsiTIGR01974 NDH_I_L, 1 hit

Sequencei

Sequence statusi: Complete.

P33607-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNMLALTIIL PLIGFVLLAF SRGRWSENVS AIVGVGSVGL AALVTAFIGV
60 70 80 90 100
DFFANGEQTY SQPLWTWMSV GDFNIGFNLV LDGLSLTMLS VVTGVGFLIH
110 120 130 140 150
MYASWYMRGE EGYSRFFAYT NLFIASMVVL VLADNLLLMY LGWEGVGLCS
160 170 180 190 200
YLLIGFYYTD PKNGAAAMKA FVVTRVGDVF LAFALFILYN ELGTLNFREM
210 220 230 240 250
VELAPAHFAD GNNMLMWATL MLLGGAVGKS AQLPLQTWLA DAMAGPTPVS
260 270 280 290 300
ALIHAATMVT AGVYLIARTH GLFLMTPEVL HLVGIVGAVT LLLAGFAALV
310 320 330 340 350
QTDIKRVLAY STMSQIGYMF LALGVQAWDA AIFHLMTHAF FKALLFLASG
360 370 380 390 400
SVILACHHEQ NIFKMGGLRK SIPLVYLCFL VGGAALSALP LVTAGFFSKD
410 420 430 440 450
EILAGAMANG HINLMVAGLV GAFMTSLYTF RMIFIVFHGK EQIHAHAVKG
460 470 480 490 500
VTHSLPLIVL LILSTFVGAL IVPPLQGVLP QTTELAHGSM LTLEITSGVV
510 520 530 540 550
AVVGILLAAW LWLGKRTLVT SIANSAPGRL LGTWWYNAWG FDWLYDKVFV
560 570 580 590 600
KPFLGIAWLL KRDPLNSMMN IPAVLSRFAG KGLLLSENGY LRWYVASMSI
610
GAVVVLALLM VLR
Length:613
Mass (Da):66,438
Last modified:November 1, 1997 - v2
Checksum:i7B768F6D4F2668A1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39G → A in CAA48371 (PubMed:7690854).Curated1
Sequence conflicti47 – 58FIGVD…ANGEQ → LSALISSLTASK in CAA48371 (PubMed:7690854).CuratedAdd BLAST12
Sequence conflicti182A → R in CAA48371 (PubMed:7690854).Curated1
Sequence conflicti208F → L in CAA48371 (PubMed:7690854).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA Translation: CAA48371.1
U00096 Genomic DNA Translation: AAC75338.1
AP009048 Genomic DNA Translation: BAA16106.1
PIRiD64999
RefSeqiNP_416781.1, NC_000913.3
WP_001056643.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75338; AAC75338; b2278
BAA16106; BAA16106; BAA16106
GeneIDi945540
KEGGiecj:JW2273
eco:b2278
PATRICifig|1411691.4.peg.4458

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68301 Genomic DNA Translation: CAA48371.1
U00096 Genomic DNA Translation: AAC75338.1
AP009048 Genomic DNA Translation: BAA16106.1
PIRiD64999
RefSeqiNP_416781.1, NC_000913.3
WP_001056643.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP33607
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260888, 94 interactors
ComplexPortaliCPX-243 Respiratory chain complex I
DIPiDIP-10388N
IntActiP33607, 1 interactor
STRINGi316385.ECDH10B_2440

Protein family/group databases

TCDBi3.D.1.1.1 the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family

Proteomic databases

PaxDbiP33607
PRIDEiP33607

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75338; AAC75338; b2278
BAA16106; BAA16106; BAA16106
GeneIDi945540
KEGGiecj:JW2273
eco:b2278
PATRICifig|1411691.4.peg.4458

Organism-specific databases

EchoBASEiEB2016
EcoGeneiEG12092 nuoL

Phylogenomic databases

eggNOGiENOG4105D65 Bacteria
COG1009 LUCA
HOGENOMiHOG000100570
InParanoidiP33607
KOiK00341
OMAiQFYALIV
PhylomeDBiP33607

Enzyme and pathway databases

BioCyciEcoCyc:NUOL-MONOMER
MetaCyc:NUOL-MONOMER

Miscellaneous databases

PROiPR:P33607

Family and domain databases

InterProiView protein in InterPro
IPR003945 NADHpl_OxRdtase_5
IPR018393 NADHpl_OxRdtase_5_subgr
IPR001750 ND/Mrp_mem
IPR001516 Proton_antipo_N
PfamiView protein in Pfam
PF00361 Proton_antipo_M, 1 hit
PF00662 Proton_antipo_N, 1 hit
PRINTSiPR01435 NPOXDRDTASE5
TIGRFAMsiTIGR01974 NDH_I_L, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNUOL_ECOLI
AccessioniPrimary (citable) accession number: P33607
Secondary accession number(s): P78254
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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