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Q9X024 (NNR_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional NAD(P)H-hydrate repair enzyme Nnr
Alternative name(s):
Nicotinamide nucleotide repair protein

Including the following 2 domains:

  1. ADP-dependent (S)-NAD(P)H-hydrate dehydratase
    EC=4.2.1.136
    Alternative name(s):
    ADP-dependent NAD(P)HX dehydratase
  2. NAD(P)H-hydrate epimerase
    EC=5.1.99.6
    Alternative name(s):
    NAD(P)HX epimerase
Gene names
Name:nnr
Ordered Locus Names:TM_0922
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga ›

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01965

Catalytic activity

ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + NADH. HAMAP-Rule MF_01965

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. HAMAP-Rule MF_01965

(6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate.

Cofactor

Binds 1 potassium ion per subunit By similarity. HAMAP-Rule MF_01965

Sequence similarities

In the N-terminal section; belongs to the nnrE/AIBP family.

In the C-terminal section; belongs to the nnrD/CARKD family.

Contains 1 YjeF C-terminal domain.

Contains 1 YjeF N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Bifunctional NAD(P)H-hydrate repair enzyme Nnr HAMAP-Rule MF_01965
PRO_0000416413

Regions

Domain1 – 204204YjeF N-terminal
Domain212 – 488277YjeF C-terminal
Nucleotide binding402 – 4065ADP HAMAP-Rule MF_01965
Nucleotide binding421 – 43010ADP HAMAP-Rule MF_01965
Region1 – 204204NAD(P)H-hydrate epimerase By similarity
Region51 – 555NAD(P)HX (for epimerase activity) HAMAP-Rule MF_01965
Region118 – 1247NAD(P)HX (for epimerase activity) HAMAP-Rule MF_01965
Region212 – 490279ADP-dependent (S)-NAD(P)H-hydrate dehydratase By similarity
Region366 – 3727NAD(P)HX (for dehydratase activity) HAMAP-Rule MF_01965

Sites

Metal binding521Potassium
Metal binding1141Potassium
Metal binding1501Potassium
Binding site1291NAD(P)HX (for epimerase activity)
Binding site1471NAD(P)HX (for epimerase activity)
Binding site3171NAD(P)HX (for dehydratase activity); via amide nitrogen
Binding site4311NAD(P)HX (for dehydratase activity)

Secondary structure

1 .............................................................................................. 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X024 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 580917C98F8BE2FC

FASTA49053,004
        10         20         30         40         50         60 
MKEIDELTIK EYGVDSRILM ERAGISVVLA MEEELGNLSD YRFLVLCGGG NNGGDGFVVA 

        70         80         90        100        110        120 
RNLLGVVKDV LVVFLGKKKT PDCEYNYGLY KKFGGKVVEQ FEPSILNEFD VVVDAIFGTG 

       130        140        150        160        170        180 
LRGEITGEYA EIINLVNKSG KVVVSVDVPS GIDSNTGKVL RTAVKADLTV TFGVPKIGHI 

       190        200        210        220        230        240 
LFPGRDLTGK LKVANIGHPV HLINSINRYV ITREMVRSLL PERPRDSHKG TYGKVLIIAG 

       250        260        270        280        290        300 
SRLYSGAPVL SGMGSLKVGT GLVKLAVPFP QNLIATSRFP ELISVPIDTE KGFFSLQNLQ 

       310        320        330        340        350        360 
ECLELSKDVD VVAIGPGLGN NEHVREFVNE FLKTLEKPAV IDADAINVLD TSVLKERKSP 

       370        380        390        400        410        420 
AVLTPHPGEM ARLVKKTVGD VKYNYELAEE FAKENDCVLV LKSATTIVTD GEKTLFNITG 

       430        440        450        460        470        480 
NTGLSKGGSG DVLTGMIAGF IAQGLSPLEA STVSVYLHGF AAELFEQDER GLTASELLRL 

       490 
IPEAIRRLKE

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of hypothetical protein (tm0922) from Thermotoga maritima at 2.27 A resolution."
Joint Center for Structural Genomics (JCSG)
Submitted (SEP-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
[3]"Identification of unknown protein function using metabolite cocktail screening."
Shumilin I.A., Cymborowski M., Lesley S.A., Minor W.
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH POTASSIUM AND SUBSTRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD36003.1.
PIRC72317.
RefSeqNP_228730.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9X024.
SMRQ9X024. Positions 1-489.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59950N.
STRING243274.TM0922.

Protocols and materials databases

DNASU898596.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36003; AAD36003; TM_0922.
GeneID898596.
KEGGtma:TM0922.
PATRIC23936775. VBITheMar51294_0936.

Phylogenomic databases

OMALVDMEVY.
ProtClustDBCLSK875475.

Enzyme and pathway databases

BioCycTMAR243274:GC6P-952-MONOMER.

Family and domain databases

Gene3D3.40.50.10260. 1 hit.
HAMAPMF_01965. NADHX_dehydratase. Fused.
MF_01966. NADHX_epimerase. Fused.
InterProIPR017953. Carbohydrate_kinase_pred_CS.
IPR026599. NnrD/CARKD.
IPR026600. NnrE/AIBP.
IPR000631. YjeF_C_carb_kinase-rel.
IPR004443. YjeF_N_dom.
[Graphical view]
PfamPF01256. Carb_kinase. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMSSF64153. YjeF_N. 1 hit.
TIGRFAMsTIGR00196. yjeF_cterm. 1 hit.
TIGR00197. yjeF_nterm. 1 hit.
PROSITEPS01049. YJEF_C_1. 1 hit.
PS01050. YJEF_C_2. 1 hit.
PS51383. YJEF_C_3. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9X024.

Entry information

Entry nameNNR_THEMA
AccessionPrimary (citable) accession number: Q9X024
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: November 1, 1999
Last modified: May 29, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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