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Protein

ADP-dependent (S)-NAD(P)H-hydrate dehydratase

Gene

nnrD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041NAD(P)HX; via amide nitrogen
Binding sitei216 – 2161NAD(P)HX

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1905ADPUniRule annotation1 Publication
Nucleotide bindingi206 – 21510ADPUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

ATP-binding, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU38720-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-dependent (S)-NAD(P)H-hydrate dehydrataseUniRule annotation (EC:4.2.1.136UniRule annotation)
Alternative name(s):
ADP-dependent NAD(P)HX dehydrataseUniRule annotation
Gene namesi
Name:nnrDUniRule annotation
Synonyms:yxkO
Ordered Locus Names:BSU38720
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276ADP-dependent (S)-NAD(P)H-hydrate dehydratasePRO_0000119046Add
BLAST

Proteomic databases

PaxDbiP94368.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

Protein-protein interaction databases

DIPiDIP-59951N.
STRINGi224308.Bsubs1_010100020896.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 147Combined sources
Helixi24 – 274Combined sources
Beta strandi29 – 335Combined sources
Beta strandi37 – 393Combined sources
Helixi41 – 5111Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 627Combined sources
Turni64 – 663Combined sources
Helixi67 – 704Combined sources
Turni71 – 733Combined sources
Beta strandi78 – 814Combined sources
Helixi83 – 864Combined sources
Turni87 – 893Combined sources
Beta strandi97 – 1015Combined sources
Helixi109 – 11810Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1273Combined sources
Helixi129 – 1313Combined sources
Beta strandi144 – 1463Combined sources
Helixi150 – 1578Combined sources
Helixi161 – 1644Combined sources
Helixi168 – 17912Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi199 – 2013Combined sources
Helixi207 – 2093Combined sources
Helixi214 – 22815Combined sources
Helixi232 – 25322Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 27414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KYHX-ray1.60A1-276[»]
3RPHX-ray1.75A1-276[»]
3RPZX-ray1.51A1-276[»]
3RQ2X-ray1.80A1-276[»]
3RQ5X-ray1.70A1-276[»]
3RQ6X-ray1.65A1-276[»]
3RQ8X-ray1.90A1-276[»]
3RQHX-ray1.75A1-276[»]
3RQQX-ray1.60A1-276[»]
3RQXX-ray1.60A1-276[»]
ProteinModelPortaliP94368.
SMRiP94368. Positions 2-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94368.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 275269YjeF C-terminalUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1557NAD(P)HX

Sequence similaritiesi

Belongs to the NnrD/CARKD family.UniRule annotation
Contains 1 YjeF C-terminal domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0063. LUCA.
HOGENOMiHOG000024581.
InParanoidiP94368.
KOiK17758.
OMAiCVNSGAG.
PhylomeDBiP94368.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01965. NADHX_dehydratase. 1 hit.
InterProiIPR017953. Carbohydrate_kinase_pred_CS.
IPR000631. CARKD.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF01256. Carb_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00196. yjeF_cterm. 1 hit.
PROSITEiPS01049. YJEF_C_1. 1 hit.
PS01050. YJEF_C_2. 1 hit.
PS51383. YJEF_C_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVPFWTEEH VRATLPERDA ESHKGTYGTA LLLAGSDDMP GAALLAGLGA
60 70 80 90 100
MRSGLGKLVI GTSENVIPLI VPVLPEATYW RDGWKKAADA QLEETYRAIA
110 120 130 140 150
IGPGLPQTES VQQAVDHVLT ADCPVILDAG ALAKRTYPKR EGPVILTPHP
160 170 180 190 200
GEFFRMTGVP VNELQKKRAE YAKEWAAQLQ TVIVLKGNQT VIAFPDGDCW
210 220 230 240 250
LNPTGNGALA KGGTGDTLTG MILGMLCCHE DPKHAVLNAV YLHGACAELW
260 270
TDEHSAHTLL AHELSDILPR VWKRFE
Length:276
Mass (Da):29,870
Last modified:May 1, 1997 - v1
Checksum:i68C14E747419478A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83026 Genomic DNA. Translation: BAA11731.1.
AL009126 Genomic DNA. Translation: CAB15898.1.
PIRiD70081.
RefSeqiNP_391751.1. NC_000964.3.
WP_003244033.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15898; CAB15898; BSU38720.
GeneIDi937408.
KEGGibsu:BSU38720.
PATRICi18979792. VBIBacSub10457_4058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83026 Genomic DNA. Translation: BAA11731.1.
AL009126 Genomic DNA. Translation: CAB15898.1.
PIRiD70081.
RefSeqiNP_391751.1. NC_000964.3.
WP_003244033.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KYHX-ray1.60A1-276[»]
3RPHX-ray1.75A1-276[»]
3RPZX-ray1.51A1-276[»]
3RQ2X-ray1.80A1-276[»]
3RQ5X-ray1.70A1-276[»]
3RQ6X-ray1.65A1-276[»]
3RQ8X-ray1.90A1-276[»]
3RQHX-ray1.75A1-276[»]
3RQQX-ray1.60A1-276[»]
3RQXX-ray1.60A1-276[»]
ProteinModelPortaliP94368.
SMRiP94368. Positions 2-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59951N.
STRINGi224308.Bsubs1_010100020896.

Proteomic databases

PaxDbiP94368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15898; CAB15898; BSU38720.
GeneIDi937408.
KEGGibsu:BSU38720.
PATRICi18979792. VBIBacSub10457_4058.

Phylogenomic databases

eggNOGiENOG4105DR1. Bacteria.
COG0063. LUCA.
HOGENOMiHOG000024581.
InParanoidiP94368.
KOiK17758.
OMAiCVNSGAG.
PhylomeDBiP94368.

Enzyme and pathway databases

BioCyciBSUB:BSU38720-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP94368.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01965. NADHX_dehydratase. 1 hit.
InterProiIPR017953. Carbohydrate_kinase_pred_CS.
IPR000631. CARKD.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF01256. Carb_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00196. yjeF_cterm. 1 hit.
PROSITEiPS01049. YJEF_C_1. 1 hit.
PS01050. YJEF_C_2. 1 hit.
PS51383. YJEF_C_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNNRD_BACSU
AccessioniPrimary (citable) accession number: P94368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: September 7, 2016
This is version 117 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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.