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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Potassium
Metal bindingi114 – 1141Potassium
Binding sitei129 – 1291NAD(P)HX (for epimerase activity)
Binding sitei147 – 1471NAD(P)HX (for epimerase activity)
Metal bindingi150 – 1501Potassium
Binding sitei317 – 3171NAD(P)HX (for dehydratase activity); via amide nitrogen
Binding sitei431 – 4311NAD(P)HX (for dehydratase activity)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi402 – 4065ADP
Nucleotide bindingi421 – 43010ADP

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

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-952-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: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Bifunctional NAD(P)H-hydrate repair enzyme NnrPRO_0000416413Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-59950N.
STRINGi243274.TM0922.

Structurei

Secondary structure

1
490
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 109Combined sources
Helixi16 – 3520Combined sources
Helixi38 – 403Combined sources
Beta strandi42 – 476Combined sources
Helixi51 – 6313Combined sources
Turni64 – 663Combined sources
Beta strandi67 – 748Combined sources
Helixi81 – 9212Combined sources
Beta strandi97 – 1004Combined sources
Helixi103 – 1086Combined sources
Beta strandi110 – 1167Combined sources
Helixi127 – 13812Combined sources
Beta strandi142 – 1487Combined sources
Turni154 – 1563Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi167 – 1748Combined sources
Helixi177 – 1804Combined sources
Helixi184 – 1885Combined sources
Beta strandi190 – 1945Combined sources
Helixi200 – 2034Combined sources
Beta strandi207 – 2104Combined sources
Helixi213 – 2197Combined sources
Helixi229 – 2324Combined sources
Beta strandi234 – 2385Combined sources
Helixi247 – 25711Combined sources
Beta strandi261 – 2688Combined sources
Turni269 – 2724Combined sources
Helixi273 – 2786Combined sources
Beta strandi282 – 2876Combined sources
Beta strandi290 – 2934Combined sources
Helixi296 – 2983Combined sources
Helixi299 – 3068Combined sources
Beta strandi310 – 3145Combined sources
Helixi322 – 33413Combined sources
Beta strandi339 – 3413Combined sources
Helixi343 – 3475Combined sources
Helixi351 – 3566Combined sources
Beta strandi361 – 3633Combined sources
Helixi367 – 3748Combined sources
Helixi378 – 3814Combined sources
Helixi385 – 39511Combined sources
Beta strandi397 – 4015Combined sources
Beta strandi403 – 4097Combined sources
Beta strandi414 – 4174Combined sources
Helixi422 – 4243Combined sources
Helixi429 – 44214Combined sources
Helixi447 – 46317Combined sources
Helixi469 – 4713Combined sources
Helixi474 – 48815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X024.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 204204YjeF N-terminalAdd
BLAST
Domaini212 – 488277YjeF C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 204204NAD(P)H-hydrate epimeraseBy similarityAdd
BLAST
Regioni51 – 555NAD(P)HX (for epimerase activity)
Regioni118 – 1247NAD(P)HX (for epimerase activity)
Regioni212 – 490279ADP-dependent (S)-NAD(P)H-hydrate dehydrataseBy similarityAdd
BLAST
Regioni366 – 3727NAD(P)HX (for dehydratase activity)

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

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
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. Positions 1-489.
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.

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-952-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9X024.

Family and domain databases

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: September 7, 2016
This is version 87 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.