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Protein

NADH-quinone oxidoreductase subunit L

Gene

nuoL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Ubiquinone

Enzyme and pathway databases

BioCyciEcoCyc:NUOL-MONOMER.
ECOL316407:JW2273-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

  • integral component of plasma membrane Source: EcoCyc
  • NADH dehydrogenase complex Source: EcoliWiki
  • plasma membrane Source: EcoCyc
  • plasma membrane respiratory chain complex I Source: EcoCyc
Complete GO annotation...

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. 12 interactors.
DIPiDIP-10388N.
STRINGi511145.b2278.

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.
OMAiAWEGAIF.
PhylomeDBiP33607.

Family and domain databases

InterProiIPR003945. NADHpl_OxRdtase_5.
IPR018393. NADHpl_OxRdtase_5_subgr.
IPR001750. ND/Mrp_mem.
IPR001516. Proton_antipo_N.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
PF00662. Proton_antipo_N. 1 hit.
[Graphical view]
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.
PATRICi32119923. VBIEscCol129921_2371.

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. 12 interactors.
DIPiDIP-10388N.
STRINGi511145.b2278.

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.
PATRICi32119923. VBIEscCol129921_2371.

Organism-specific databases

EchoBASEiEB2016.
EcoGeneiEG12092. nuoL.

Phylogenomic databases

eggNOGiENOG4105D65. Bacteria.
COG1009. LUCA.
HOGENOMiHOG000100570.
InParanoidiP33607.
KOiK00341.
OMAiAWEGAIF.
PhylomeDBiP33607.

Enzyme and pathway databases

BioCyciEcoCyc:NUOL-MONOMER.
ECOL316407:JW2273-MONOMER.
MetaCyc:NUOL-MONOMER.

Miscellaneous databases

PROiP33607.

Family and domain databases

InterProiIPR003945. NADHpl_OxRdtase_5.
IPR018393. NADHpl_OxRdtase_5_subgr.
IPR001750. ND/Mrp_mem.
IPR001516. Proton_antipo_N.
[Graphical view]
PfamiPF00361. Proton_antipo_M. 1 hit.
PF00662. Proton_antipo_N. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.