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P32664 (NUDC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH pyrophosphatase
EC=3.6.1.22
Gene names
Name:nudC
Synonyms:yjaD
Ordered Locus Names:b3996, JW5548
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

NAD+ + H2O = AMP + NMN. Ref.6

Cofactor

Divalent metal cations. Magnesium or manganese. Ref.6

Binds 1 zinc ion per subunit. Ref.6

Subunit structure

Homodimer Probable. Ref.6

Sequence similarities

Belongs to the Nudix hydrolase family. NudC subfamily.

Contains 1 nudix hydrolase domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.5. HAMAP-Rule MF_00297

Sequence caution

The sequence D12624 differs from that shown. Reason: Frameshift at position 116.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257NADH pyrophosphatase HAMAP-Rule MF_00297
PRO_0000056963

Regions

Domain125 – 248124Nudix hydrolase
Motif159 – 18022Nudix box HAMAP-Rule MF_00297

Sites

Metal binding981Zinc
Metal binding1011Zinc
Metal binding1161Zinc
Metal binding1191Zinc
Metal binding1741Divalent metal cation By similarity
Metal binding1781Divalent metal cation By similarity

Experimental info

Sequence conflict331A → R in AAC43094. Ref.2

Secondary structure

1 .......................................... 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32664 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 368FAE0480AF4CB3

FASTA25729,689
        10         20         30         40         50         60 
MDRIIEKLDH GWWVVSHEQK LWLPKGELPY GEAANFDLVG QRALQIGEWQ GEPVWLVQQQ 

        70         80         90        100        110        120 
RRHDMGSVRQ VIDLDVGLFQ LAGRGVQLAE FYRSHKYCGY CGHEMYPSKT EWAMLCSHCR 

       130        140        150        160        170        180 
ERYYPQIAPC IIVAIRRDDS ILLAQHTRHR NGVHTVLAGF VEVGETLEQA VAREVMEESG 

       190        200        210        220        230        240 
IKVKNLRYVT SQPWPFPQSL MTAFMAEYDS GDIVIDPKEL LEANWYRYDD LPLLPPPGTV 

       250 
ARRLIEDTVA MCRAEYE

« Hide

References

« Hide 'large scale' references
[1]Nishimura K., Inokuchi H.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 33.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Cloning, purification, and properties of a novel NADH pyrophosphatase. Evidence for a nucleotide pyrophosphatase catalytic domain in MutT-like enzymes."
Frick D.N., Bessman M.J.
J. Biol. Chem. 270:1529-1534(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
Strain: K12 / MG1655 / ATCC 47076.
[7]"Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli K12 at 2.20 A resolution."
Joint center for structural genomics (JCSG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D12624 Genomic DNA. No translation available.
U00006 Genomic DNA. Translation: AAC43094.1.
U00096 Genomic DNA. Translation: AAT48238.1.
AP009048 Genomic DNA. Translation: BAE77323.1.
PIRG65206.
RefSeqYP_026280.1. NC_000913.2.
YP_491464.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VK6X-ray2.20A1-257[»]
2GB5X-ray2.30A/B1-257[»]
ProteinModelPortalP32664.
SMRP32664. Positions 1-256.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10373N.
IntActP32664. 1 interaction.
STRING511145.b3996.

Proteomic databases

PaxDbP32664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48238; AAT48238; b3996.
BAE77323; BAE77323; BAE77323.
GeneID12934221.
948498.
KEGGecj:Y75_p3200.
eco:b3996.
PATRIC32123515. VBIEscCol129921_4110.

Organism-specific databases

EchoBASEEB1653.
EcoGeneEG11702. nudC.

Phylogenomic databases

eggNOGCOG2816.
HOGENOMHOG000247937.
KOK03426.
OMATELACLC.
ProtClustDBPRK00241.

Enzyme and pathway databases

BioCycEcoCyc:EG11702-MONOMER.
ECOL316407:JW5548-MONOMER.
MetaCyc:EG11702-MONOMER.

Gene expression databases

GenevestigatorP32664.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
HAMAPMF_00297. Nudix_NudC.
InterProIPR015375. NADH_PPase-like_N.
IPR022925. NADH_pyroPase_NudC.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR015376. Znr_NADH_PPase.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
PF09296. NUDIX-like. 1 hit.
PF09297. zf-NADH-PPase. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 2 hits.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32664.

Entry information

Entry nameNUDC_ECOLI
AccessionPrimary (citable) accession number: P32664
Secondary accession number(s): Q2M8T3, Q6BEX6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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