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Protein

Bifunctional NAD(P)H-hydrate repair enzyme Nnr

Gene

nnr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.1 Publication

Catalytic activityi

ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + NADH.1 Publication
ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + phosphate + NADPH.1 Publication
(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide.1 Publication
(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate.1 Publication

Cofactori

K+By similarityNote: Binds 1 potassium ion per subunit.By similarity

Kineticsi

  1. KM=1.2 µM for (S)-NADHX1 Publication
  2. KM=0.86 µM for (S)-NADPHX1 Publication
  3. KM=3.6 µM for ADP1 Publication
  1. Vmax=0.62 µmol/min/mg enzyme toward (S)-NADHX1 Publication
  2. Vmax=0.88 µmol/min/mg enzyme toward (S)-NADPHX1 Publication
  3. Vmax=0.6 µmol/min/mg enzyme toward ADP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi72PotassiumBy similarity1
Metal bindingi135PotassiumBy similarity1
Binding sitei168NAD(P)HX (for epimerase activity)By similarity1
Metal bindingi171PotassiumBy similarity1
Binding sitei329NAD(P)HX (for dehydratase activity); via amide nitrogenBy similarity1
Binding sitei442NAD(P)HX (for dehydratase activity)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi412 – 416ADPBy similarity5
Nucleotide bindingi432 – 441ADPBy similarity10

GO - Molecular functioni

  • ADP-dependent NAD(P)H-hydrate dehydratase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • NADHX epimerase activity Source: EcoCyc
  • NADPHX epimerase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

ATP-binding, Metal-binding, NAD, NADP, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:EG11758-MONOMER.
ECOL316407:JW4125-MONOMER.
MetaCyc:EG11758-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional NAD(P)H-hydrate repair enzyme Nnr
Alternative name(s):
Nicotinamide nucleotide repair protein
Including the following 2 domains:
ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC:4.2.1.136)
Alternative name(s):
ADP-dependent NAD(P)HX dehydratase
NAD(P)H-hydrate epimerase (EC:5.1.99.6)
Alternative name(s):
NAD(P)HX epimerase
Gene namesi
Name:nnr
Synonyms:yjeF
Ordered Locus Names:b4167, JW4125
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11758. yjeF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190431 – 515Bifunctional NAD(P)H-hydrate repair enzyme NnrAdd BLAST515

Proteomic databases

PaxDbiP31806.
PRIDEiP31806.

Interactioni

Protein-protein interaction databases

BioGridi4262704. 118 interactors.
DIPiDIP-12572N.
IntActiP31806. 9 interactors.
MINTiMINT-1242763.
STRINGi511145.b4167.

Structurei

3D structure databases

ProteinModelPortaliP31806.
SMRiP31806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 225YjeF N-terminalAdd BLAST203
Domaini234 – 501YjeF C-terminalAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 227NAD(P)H-hydrate epimeraseBy similarityAdd BLAST227
Regioni71 – 75NAD(P)HX (for epimerase activity)By similarity5
Regioni139 – 145NAD(P)HX (for epimerase activity)By similarity7
Regioni235 – 515ADP-dependent (S)-NAD(P)H-hydrate dehydrataseBy similarityAdd BLAST281
Regioni375 – 381NAD(P)HX (for dehydratase activity)By similarity7

Sequence similaritiesi

In the N-terminal section; belongs to the NnrE/AIBP family.Curated
In the C-terminal section; belongs to the NnrD/CARKD family.Curated
Contains 1 YjeF C-terminal domain.Curated
Contains 1 YjeF N-terminal domain.Curated

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
HOGENOMiHOG000228406.
InParanoidiP31806.
KOiK17758.
K17759.
OMAiKGDHGRV.
PhylomeDBiP31806.

Family and domain databases

CDDicd01171. YXKO-related. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
3.40.50.10260. 1 hit.
HAMAPiMF_01965. NADHX_dehydratase. 1 hit.
MF_01966. NADHX_epimerase. 1 hit.
InterProiIPR017953. Carbohydrate_kinase_pred_CS.
IPR000631. CARKD.
IPR030677. Nnr.
IPR029056. Ribokinase-like.
IPR004443. YjeF_N_dom.
[Graphical view]
PfamiPF01256. Carb_kinase. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017184. Nnr. 1 hit.
SUPFAMiSSF53613. SSF53613. 1 hit.
SSF64153. SSF64153. 1 hit.
TIGRFAMsiTIGR00196. yjeF_cterm. 1 hit.
TIGR00197. yjeF_nterm. 1 hit.
PROSITEiPS01049. YJEF_C_1. 1 hit.
PS01050. YJEF_C_2. 1 hit.
PS51383. YJEF_C_3. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31806-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDHTMKKNP VSIPHTVWYA DDIRRGEREA ADVLGLTLYE LMLRAGEAAF
60 70 80 90 100
QVCRSAYPDA RHWLVLCGHG NNGGDGYVVA RLAKAVGIEV TLLAQESDKP
110 120 130 140 150
LPEEAALARE AWLNAGGEIH ASNIVWPESV DLIVDALLGT GLRQAPRESI
160 170 180 190 200
SQLIDHANSH PAPIVAVDIP SGLLAETGAT PGAVINADHT ITFIALKPGL
210 220 230 240 250
LTGKARDVTG QLHFDSLGLD SWLAGQETKI QRFSAEQLSH WLKPRRPTSH
260 270 280 290 300
KGDHGRLVII GGDHGTAGAI RMTGEAALRA GAGLVRVLTR SENIAPLLTA
310 320 330 340 350
RPELMVHELT MDSLTESLEW ADVVVIGPGL GQQEWGKKAL QKVENFRKPM
360 370 380 390 400
LWDADALNLL AINPDKRHNR VITPHPGEAA RLLGCSVAEI ESDRLHCAKR
410 420 430 440 450
LVQRYGGVAV LKGAGTVVAA HPDALGIIDA GNAGMASGGM GDVLSGIIGA
460 470 480 490 500
LLGQKLSPYD AACAGCVAHG AAADVLAARF GTRGMLATDL FSTLQRIVNP
510
EVTDKNHDES SNSAP
Length:515
Mass (Da):54,650
Last modified:February 1, 1995 - v2
Checksum:i007D569D11E11530
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97063.1.
U00096 Genomic DNA. Translation: AAC77124.1.
AP009048 Genomic DNA. Translation: BAE78168.1.
L19346 Unassigned DNA. Translation: AAA20095.1.
PIRiS56392.
RefSeqiNP_418588.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77124; AAC77124; b4167.
BAE78168; BAE78168; BAE78168.
GeneIDi948685.
KEGGiecj:JW4125.
eco:b4167.
PATRICi32123907. VBIEscCol129921_4298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97063.1.
U00096 Genomic DNA. Translation: AAC77124.1.
AP009048 Genomic DNA. Translation: BAE78168.1.
L19346 Unassigned DNA. Translation: AAA20095.1.
PIRiS56392.
RefSeqiNP_418588.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP31806.
SMRiP31806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262704. 118 interactors.
DIPiDIP-12572N.
IntActiP31806. 9 interactors.
MINTiMINT-1242763.
STRINGi511145.b4167.

Proteomic databases

PaxDbiP31806.
PRIDEiP31806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77124; AAC77124; b4167.
BAE78168; BAE78168; BAE78168.
GeneIDi948685.
KEGGiecj:JW4125.
eco:b4167.
PATRICi32123907. VBIEscCol129921_4298.

Organism-specific databases

EchoBASEiEB1708.
EcoGeneiEG11758. yjeF.

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
HOGENOMiHOG000228406.
InParanoidiP31806.
KOiK17758.
K17759.
OMAiKGDHGRV.
PhylomeDBiP31806.

Enzyme and pathway databases

BioCyciEcoCyc:EG11758-MONOMER.
ECOL316407:JW4125-MONOMER.
MetaCyc:EG11758-MONOMER.

Miscellaneous databases

PROiP31806.

Family and domain databases

CDDicd01171. YXKO-related. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
3.40.50.10260. 1 hit.
HAMAPiMF_01965. NADHX_dehydratase. 1 hit.
MF_01966. NADHX_epimerase. 1 hit.
InterProiIPR017953. Carbohydrate_kinase_pred_CS.
IPR000631. CARKD.
IPR030677. Nnr.
IPR029056. Ribokinase-like.
IPR004443. YjeF_N_dom.
[Graphical view]
PfamiPF01256. Carb_kinase. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017184. Nnr. 1 hit.
SUPFAMiSSF53613. SSF53613. 1 hit.
SSF64153. SSF64153. 1 hit.
TIGRFAMsiTIGR00196. yjeF_cterm. 1 hit.
TIGR00197. yjeF_nterm. 1 hit.
PROSITEiPS01049. YJEF_C_1. 1 hit.
PS01050. YJEF_C_2. 1 hit.
PS51383. YJEF_C_3. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNNR_ECOLI
AccessioniPrimary (citable) accession number: P31806
Secondary accession number(s): Q2M6D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 131 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, Multifunctional enzyme, 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
  3. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.