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Protein

Bifunctional NAD(P)H-hydrate repair enzyme Nnr

Gene

nnr

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi63PotassiumBy similarity1
Metal bindingi119PotassiumBy similarity1
Binding sitei152NAD(P)HX (for epimerase activity)By similarity1
Metal bindingi155PotassiumBy similarity1
Binding sitei298NAD(P)HX (for dehydratase activity); via amide nitrogenBy similarity1
Binding sitei412NAD(P)HX (for dehydratase activity)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi382 – 386ADPBy similarity5
Nucleotide bindingi402 – 411ADPBy similarity10

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

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

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
Ordered Locus Names:ML0373
ORF Names:B229_C2_201, u229g
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190471 – 473Bifunctional NAD(P)H-hydrate repair enzyme NnrAdd BLAST473

Interactioni

Protein-protein interaction databases

STRINGi272631.ML0373.

Structurei

3D structure databases

ProteinModelPortaliP37391.
SMRiP37391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 205YjeF N-terminalAdd BLAST196
Domaini210 – 473YjeF C-terminalAdd BLAST264

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 203NAD(P)H-hydrate epimeraseBy similarityAdd BLAST203
Regioni62 – 66NAD(P)HX (for epimerase activity)By similarity5
Regioni123 – 129NAD(P)HX (for epimerase activity)By similarity7
Regioni210 – 473ADP-dependent (S)-NAD(P)H-hydrate dehydrataseBy similarityAdd BLAST264
Regioni348 – 354NAD(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

eggNOGiENOG4107QTJ. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
HOGENOMiHOG000228405.
OMAiKGDHGRV.
OrthoDBiPOG091H01XZ.

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.

P37391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHYYSVAAI RDAEASLLAS LPDGVLMKRA AYGLASVIIR ELAVRTGGVT
60 70 80 90 100
GRRVCAVVGS GDNGGDALWA ATFLRRRGAA ADAVLLNPDR VHRKALVAFR
110 120 130 140 150
KAGGRIVENV SAATDLVIDG VVGISGSGPL RPAAAAVFAT VSASGVPVVA
160 170 180 190 200
VDLPSGIDVV TGVINGPAVH AALTVTFGGL KPVHALADCG DVTLVDIGLD
210 220 230 240 250
LPDSDILGLQ AADVAAYWPV PGVHDDKYTQ GVTGVLAGSS TYPGAAVLCT
260 270 280 290 300
GAAVAATSGM VRYAGSAYTQ VLAHWPEVIA SATPTAAGRV QSWVVGPGLG
310 320 330 340 350
IDATATAALW FALETDLPVL VDADGLTMLA AHPDLVINRN APTVLTPHAS
360 370 380 390 400
EFARLAGTPP GDDRVGACRK LADSFGATVL LKGNVTVIAD PGGPVYLNPA
410 420 430 440 450
GQSWAATAGS GDVLSGMIGA LLAAGLPAAE AAAAAAFVHA RAAALSAADP
460 470
GPGDVPTSAS RMVSHIRTAL AAL
Length:473
Mass (Da):47,227
Last modified:April 27, 2001 - v2
Checksum:i29569CBBD666C81C
GO

Sequence cautioni

The sequence AAA17298 differs from that shown. Reason: Frameshift at positions 76 and 429.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66 – 67DA → ES (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00020 Genomic DNA. Translation: AAA17298.1. Frameshift.
AL583918 Genomic DNA. Translation: CAC29881.1.
PIRiE86955.
S72984.
RefSeqiNP_301366.1. NC_002677.1.
WP_010907690.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC29881; CAC29881; CAC29881.
GeneIDi909029.
KEGGimle:ML0373.
PATRICi18051362. VBIMycLep78757_0630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00020 Genomic DNA. Translation: AAA17298.1. Frameshift.
AL583918 Genomic DNA. Translation: CAC29881.1.
PIRiE86955.
S72984.
RefSeqiNP_301366.1. NC_002677.1.
WP_010907690.1. NC_002677.1.

3D structure databases

ProteinModelPortaliP37391.
SMRiP37391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC29881; CAC29881; CAC29881.
GeneIDi909029.
KEGGimle:ML0373.
PATRICi18051362. VBIMycLep78757_0630.

Organism-specific databases

LepromaiML0373.

Phylogenomic databases

eggNOGiENOG4107QTJ. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
HOGENOMiHOG000228405.
OMAiKGDHGRV.
OrthoDBiPOG091H01XZ.

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_MYCLE
AccessioniPrimary (citable) accession number: P37391
Secondary accession number(s): Q9CCV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 27, 2001
Last modified: November 2, 2016
This is version 108 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. 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.