nnr

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	57	PotassiumBy similarity	1
Metal bindingⁱ	120	PotassiumBy similarity	1
Binding siteⁱ	151	NAD(P)HX (for epimerase activity)By similarity	1
Metal bindingⁱ	154	PotassiumBy similarity	1
Binding siteⁱ	300	NAD(P)HX (for dehydratase activity); via amide nitrogenBy similarity	1
Binding siteⁱ	414	NAD(P)HX (for dehydratase activity)By similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	385 – 389	ADPBy similarity		5
Nucleotide bindingⁱ	404 – 413	ADPBy similarity		10

GO - Molecular functionⁱ

ADP-dependent NAD(P)H-hydrate dehydratase activity Source: InterPro
ATP binding Source: UniProtKB-KW
isomerase activity Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

metabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase, Lyase, Multifunctional enzyme
Ligand	ATP-binding, Metal-binding, NAD, NADP, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCycⁱ	HPY:HP1363-MONOMER

BioCycⁱ

HPY:HP1363-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 Ordered Locus Names:HP_1363
Organismⁱ	Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifierⁱ	85962 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori
Proteomesⁱ	UP000000429 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000119044	1 – 466	Bifunctional NAD(P)H-hydrate repair enzyme NnrAdd BLAST		466

Proteomic databases

PaxDbⁱ	P56176
PRIDEⁱ	P56176

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	85962.HP1363

STRINGⁱ

85962.HP1363

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 6	Combined sources	5
Helixⁱ	9 – 17	Combined sources	9
Helixⁱ	23 – 39	Combined sources	17
Beta strandⁱ	47 – 52	Combined sources	6
Helixⁱ	56 – 68	Combined sources	13
Beta strandⁱ	72 – 80	Combined sources	9
Helixⁱ	85 – 96	Combined sources	12
Beta strandⁱ	100 – 103	Combined sources	4
Beta strandⁱ	115 – 122	Combined sources	8
Helixⁱ	137 – 140	Combined sources	4
Turnⁱ	141 – 143	Combined sources	3
Beta strandⁱ	144 – 152	Combined sources	9
Beta strandⁱ	170 – 179	Combined sources	10
Helixⁱ	180 – 183	Combined sources	4
Helixⁱ	185 – 187	Combined sources	3
Helixⁱ	188 – 191	Combined sources	4
Beta strandⁱ	193 – 197	Combined sources	5
Helixⁱ	203 – 206	Combined sources	4
Beta strandⁱ	211 – 214	Combined sources	4
Helixⁱ	217 – 219	Combined sources	3
Helixⁱ	232 – 235	Combined sources	4
Beta strandⁱ	237 – 242	Combined sources	6
Helixⁱ	246 – 258	Combined sources	13
Beta strandⁱ	262 – 271	Combined sources	10
Beta strandⁱ	274 – 278	Combined sources	5
Beta strandⁱ	282 – 287	Combined sources	6
Beta strandⁱ	293 – 297	Combined sources	5
Helixⁱ	308 – 314	Combined sources	7
Beta strandⁱ	317 – 320	Combined sources	4
Helixⁱ	321 – 325	Combined sources	5
Helixⁱ	327 – 330	Combined sources	4
Turnⁱ	331 – 334	Combined sources	4
Beta strandⁱ	335 – 340	Combined sources	6
Helixⁱ	343 – 349	Combined sources	7
Turnⁱ	350 – 353	Combined sources	4
Helixⁱ	362 – 364	Combined sources	3
Helixⁱ	371 – 376	Combined sources	6
Beta strandⁱ	380 – 384	Combined sources	5
Beta strandⁱ	386 – 393	Combined sources	8
Beta strandⁱ	396 – 400	Combined sources	5
Helixⁱ	405 – 407	Combined sources	3
Helixⁱ	412 – 425	Combined sources	14
Helixⁱ	430 – 443	Combined sources	14
Helixⁱ	444 – 447	Combined sources	4
Helixⁱ	456 – 464	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P56176
SMRⁱ	P56176
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P56176

EvolutionaryTraceⁱ

P56176

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	8 – 207	YjeF N-terminalAdd BLAST		200
Domainⁱ	215 – 466	YjeF C-terminalAdd BLAST		252

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 207	NAD(P)H-hydrate epimeraseBy similarityAdd BLAST	207
Regionⁱ	56 – 60	NAD(P)HX (for epimerase activity)By similarity	5
Regionⁱ	124 – 130	NAD(P)HX (for epimerase activity)By similarity	7
Regionⁱ	215 – 466	ADP-dependent (S)-NAD(P)H-hydrate dehydrataseBy similarityAdd BLAST	252
Regionⁱ	342 – 348	NAD(P)HX (for dehydratase activity)By similarity	7

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

Phylogenomic databases

eggNOGⁱ	ENOG4105DR1 Bacteria COG0062 LUCA COG0063 LUCA
KEGG Orthology (KO) More...KOⁱ	K17758 K17759
OMAⁱ	KSPMCQL

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01171 YXKO-related, 1 hit
Gene3Dⁱ	3.40.1190.20, 1 hit 3.40.50.10260, 1 hit
HAMAPⁱ	MF_01965 NADHX_dehydratase, 1 hit MF_01966 NADHX_epimerase, 1 hit
InterProⁱ	View protein in InterPro IPR017953 Carbohydrate_kinase_pred_CS IPR000631 CARKD IPR030677 Nnr IPR029056 Ribokinase-like IPR004443 YjeF_N_dom IPR036652 YjeF_N_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01256 Carb_kinase, 1 hit PF03853 YjeF_N, 1 hit
PIRSFⁱ	PIRSF017184 Nnr, 1 hit
SUPFAMⁱ	SSF53613 SSF53613, 1 hit SSF64153 SSF64153, 1 hit
TIGRFAMsⁱ	TIGR00196 yjeF_cterm, 1 hit TIGR00197 yjeF_nterm, 1 hit
PROSITEⁱ	View protein in PROSITE PS01050 YJEF_C_2, 1 hit PS51383 YJEF_C_3, 1 hit PS51385 YJEF_N, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P56176-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLSVYEKVNA LDKRAIEELF LSEDILMENA AMALERAVLQ NASLGAKVII 
        60         70         80         90        100
LCGSGDNGGD GYALARRLVG RFKTLVFEMK LAKSPMCQLQ QERAKKAGVV 
       110        120        130        140        150
IKAYEENALN QNLECDVLID CVIGSHFKGK LEPFLNFESL SQKARFKIAC 
       160        170        180        190        200
DIPSGIDSKG RVDKGAFKAD LTISMGAIKS CLLSDRAKDY VGELKVGHLG 
       210        220        230        240        250
VFNQIYEIPT DTFLLEKSDL KLPLRDRKNA HKGDYGHAHV LLGKHSGAGL 
       260        270        280        290        300
LSALSALSFG SGVVSVQALE CEITSNNKPL ELVFCENFPN LLSAFALGMG 
       310        320        330        340        350
LENIPKDFNK WLELAPCVLD AGVFYHKEVL QALEKEVILT PHPKEFLSLL 
       360        370        380        390        400
KLVGINISML ELLDNKLEIA RDFSQKYPKV VLLLKGANTL IAHQGQVFIN 
       410        420        430        440        450
ILGSVALAKA GSGDVLAGLI LSLLSQNYTP LDAAINASSA HALASLEFKN 
       460 
NYALTPLDLI EKIKQL

Length:466

Mass (Da):50,737

Last modified:November 1, 1997 - v1

Checksum:ⁱ52125FE79BA8F056

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE000511 Genomic DNA Translation: AAD08403.1
PIRⁱ	C64690
NCBI Reference Sequences More...RefSeqⁱ	NP_208155.1, NC_000915.1 WP_000954017.1, NC_018939.1

Genome annotation databases

EnsemblBacteriaⁱ	AAD08403; AAD08403; HP_1363
GeneIDⁱ	900323
KEGGⁱ	heo:C694_07035 hpy:HP1363
PATRICⁱ	fig\|85962.47.peg.1460

Protein	Similar proteins		Species	Score	Length	Source
P56176	Bifunctional NAD(P)H-hydrate repair enzyme Nnr		HELPJ		464	UniRef90_P56176
Bifunctional NAD(P)H-hydrate repair enzyme		HELPX		466
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori FD703		481
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori R32b		466
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori NY40		466
+624

Protein	Similar proteins		Species	Score	Length	Source
P56176	Bifunctional NAD(P)H-hydrate repair enzyme Nnr		HELPJ		464	UniRef50_P56176
Bifunctional NAD(P)H-hydrate repair enzyme		HELPX		466
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori FD703		481
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori Hp A-9		466
Bifunctional NAD(P)H-hydrate repair enzyme		Helicobacter pylori R037c		466
+680

Entry informationⁱ

Entry nameⁱ	NNR_HELPY
Accessionⁱ	P56176Primary (citable) accession number: P56176
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 1, 1997
	Last modified:	May 23, 2018
	This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB - P56176 (NNR_HELPY)

Your basket is currently empty. ⁱ

Bifunctional NAD(P)H-hydrate repair enzyme Nnr

Select a section on the left to see content.

Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Sites

Regions

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Enzyme and pathway databases

Names & Taxonomyⁱ

PTM / Processingⁱ

Molecule processing

Proteomic databases

Interactionⁱ

Protein-protein interaction databases

Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

Family & Domainsⁱ

Domains and Repeats

Region

Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Similar proteinsⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

UniProt is an ELIXIR core data resource

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P56176 (NNR_HELPY)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Bifunctional NAD(P)H-hydrate repair enzyme Nnr

nnr

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ