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Protein

Bifunctional NAD(P)H-hydrate repair enzyme Nnr

Gene

nnr

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 (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 bindingi52Potassium1
Metal bindingi114Potassium1
Binding sitei129NAD(P)HX (for epimerase activity)1
Binding sitei147NAD(P)HX (for epimerase activity)1
Metal bindingi150Potassium1
Binding sitei317NAD(P)HX (for dehydratase activity); via amide nitrogen1
Binding sitei431NAD(P)HX (for dehydratase activity)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi402 – 406ADP5
Nucleotide bindingi421 – 430ADP10

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:TM_0922
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004164131 – 490Bifunctional NAD(P)H-hydrate repair enzyme NnrAdd BLAST490

Interactioni

Protein-protein interaction databases

DIPiDIP-59950N.
STRINGi243274.TM0922.

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 10Combined sources9
Helixi16 – 35Combined sources20
Helixi38 – 40Combined sources3
Beta strandi42 – 47Combined sources6
Helixi51 – 63Combined sources13
Turni64 – 66Combined sources3
Beta strandi67 – 74Combined sources8
Helixi81 – 92Combined sources12
Beta strandi97 – 100Combined sources4
Helixi103 – 108Combined sources6
Beta strandi110 – 116Combined sources7
Helixi127 – 138Combined sources12
Beta strandi142 – 148Combined sources7
Turni154 – 156Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi167 – 174Combined sources8
Helixi177 – 180Combined sources4
Helixi184 – 188Combined sources5
Beta strandi190 – 194Combined sources5
Helixi200 – 203Combined sources4
Beta strandi207 – 210Combined sources4
Helixi213 – 219Combined sources7
Helixi229 – 232Combined sources4
Beta strandi234 – 238Combined sources5
Helixi247 – 257Combined sources11
Beta strandi261 – 268Combined sources8
Turni269 – 272Combined sources4
Helixi273 – 278Combined sources6
Beta strandi282 – 287Combined sources6
Beta strandi290 – 293Combined sources4
Helixi296 – 298Combined sources3
Helixi299 – 306Combined sources8
Beta strandi310 – 314Combined sources5
Helixi322 – 334Combined sources13
Beta strandi339 – 341Combined sources3
Helixi343 – 347Combined sources5
Helixi351 – 356Combined sources6
Beta strandi361 – 363Combined sources3
Helixi367 – 374Combined sources8
Helixi378 – 381Combined sources4
Helixi385 – 395Combined sources11
Beta strandi397 – 401Combined sources5
Beta strandi403 – 409Combined sources7
Beta strandi414 – 417Combined sources4
Helixi422 – 424Combined sources3
Helixi429 – 442Combined sources14
Helixi447 – 463Combined sources17
Helixi469 – 471Combined sources3
Helixi474 – 488Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AX3X-ray2.27A1-490[»]
3RRBX-ray2.40A1-490[»]
3RREX-ray2.15A1-490[»]
3RRFX-ray2.10A1-490[»]
3RRJX-ray2.50A1-490[»]
3RS8X-ray2.10A1-490[»]
3RS9X-ray2.10A1-490[»]
3RSFX-ray2.30A1-490[»]
3RSGX-ray2.10A1-490[»]
3RSQX-ray2.05A1-490[»]
3RSSX-ray1.95A1-490[»]
3RT7X-ray2.10A1-490[»]
3RT9X-ray1.95A1-490[»]
3RTAX-ray1.95A1-490[»]
3RTBX-ray2.10A1-490[»]
3RTCX-ray2.10A1-490[»]
3RTDX-ray2.30A1-490[»]
3RTEX-ray2.10A1-490[»]
3RTGX-ray2.05A1-490[»]
3RU2X-ray2.20A1-490[»]
3RU3X-ray2.60A1-490[»]
ProteinModelPortaliQ9X024.
SMRiQ9X024.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X024.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 204YjeF N-terminalAdd BLAST204
Domaini212 – 488YjeF C-terminalAdd BLAST277

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 204NAD(P)H-hydrate epimeraseBy similarityAdd BLAST204
Regioni51 – 55NAD(P)HX (for epimerase activity)5
Regioni118 – 124NAD(P)HX (for epimerase activity)7
Regioni212 – 490ADP-dependent (S)-NAD(P)H-hydrate dehydrataseBy similarityAdd BLAST279
Regioni366 – 372NAD(P)HX (for dehydratase activity)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
Contains 1 YjeF C-terminal domain.Curated
Contains 1 YjeF N-terminal domain.Curated

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
InParanoidiQ9X024.
KOiK17758.
K17759.
OMAiKGDHGRV.

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.

Q9X024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEIDELTIK EYGVDSRILM ERAGISVVLA MEEELGNLSD YRFLVLCGGG
60 70 80 90 100
NNGGDGFVVA RNLLGVVKDV LVVFLGKKKT PDCEYNYGLY KKFGGKVVEQ
110 120 130 140 150
FEPSILNEFD VVVDAIFGTG LRGEITGEYA EIINLVNKSG KVVVSVDVPS
160 170 180 190 200
GIDSNTGKVL RTAVKADLTV TFGVPKIGHI LFPGRDLTGK LKVANIGHPV
210 220 230 240 250
HLINSINRYV ITREMVRSLL PERPRDSHKG TYGKVLIIAG SRLYSGAPVL
260 270 280 290 300
SGMGSLKVGT GLVKLAVPFP QNLIATSRFP ELISVPIDTE KGFFSLQNLQ
310 320 330 340 350
ECLELSKDVD VVAIGPGLGN NEHVREFVNE FLKTLEKPAV IDADAINVLD
360 370 380 390 400
TSVLKERKSP AVLTPHPGEM ARLVKKTVGD VKYNYELAEE FAKENDCVLV
410 420 430 440 450
LKSATTIVTD GEKTLFNITG NTGLSKGGSG DVLTGMIAGF IAQGLSPLEA
460 470 480 490
STVSVYLHGF AAELFEQDER GLTASELLRL IPEAIRRLKE
Length:490
Mass (Da):53,004
Last modified:November 1, 1999 - v1
Checksum:i580917C98F8BE2FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36003.1.
PIRiC72317.
RefSeqiNP_228730.1. NC_000853.1.
WP_010865220.1. NC_000853.1.

Genome annotation databases

EnsemblBacteriaiAAD36003; AAD36003; TM_0922.
GeneIDi898596.
KEGGitma:TM0922.
PATRICi23936775. VBITheMar51294_0936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36003.1.
PIRiC72317.
RefSeqiNP_228730.1. NC_000853.1.
WP_010865220.1. NC_000853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AX3X-ray2.27A1-490[»]
3RRBX-ray2.40A1-490[»]
3RREX-ray2.15A1-490[»]
3RRFX-ray2.10A1-490[»]
3RRJX-ray2.50A1-490[»]
3RS8X-ray2.10A1-490[»]
3RS9X-ray2.10A1-490[»]
3RSFX-ray2.30A1-490[»]
3RSGX-ray2.10A1-490[»]
3RSQX-ray2.05A1-490[»]
3RSSX-ray1.95A1-490[»]
3RT7X-ray2.10A1-490[»]
3RT9X-ray1.95A1-490[»]
3RTAX-ray1.95A1-490[»]
3RTBX-ray2.10A1-490[»]
3RTCX-ray2.10A1-490[»]
3RTDX-ray2.30A1-490[»]
3RTEX-ray2.10A1-490[»]
3RTGX-ray2.05A1-490[»]
3RU2X-ray2.20A1-490[»]
3RU3X-ray2.60A1-490[»]
ProteinModelPortaliQ9X024.
SMRiQ9X024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59950N.
STRINGi243274.TM0922.

Protocols and materials databases

DNASUi898596.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36003; AAD36003; TM_0922.
GeneIDi898596.
KEGGitma:TM0922.
PATRICi23936775. VBITheMar51294_0936.

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0062. LUCA.
COG0063. LUCA.
InParanoidiQ9X024.
KOiK17758.
K17759.
OMAiKGDHGRV.

Miscellaneous databases

EvolutionaryTraceiQ9X024.

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_THEMA
AccessioniPrimary (citable) accession number: Q9X024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.