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P56065 (PAND_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase
EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase

Cleaved into the following 2 chains:

  1. Aspartate 1-decarboxylase beta chain
  2. Aspartate 1-decarboxylase alpha chain
Gene names
Name:panD
Ordered Locus Names:HP_0034
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446

Catalytic activity

L-aspartate = beta-alanine + CO2. HAMAP MF_00446

Cofactor

Pyruvoyl group.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446

Subunit structure

Heterooctamer of four alpha and four beta subunits. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP MF_00446.

Post-translational modification

Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. HAMAP MF_00446

Sequence similarities

Belongs to the PanD family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandPyruvate
Schiff base
   Molecular functionDecarboxylase
Lyase
   PTMAutocatalytic cleavage
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processalanine biosynthetic process

Inferred from electronic annotation. Source: InterPro

pantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartate 1-decarboxylase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain By similarity
PRO_0000023091
Chain25 – 11793Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000023092

Regions

Region72 – 743Substrate binding HAMAP MF_00446

Sites

Active site251Schiff-base intermediate with substrate; via pyruvic acid
Active site581Proton donor
Binding site571Substrate

Amino acid modifications

Modified residue251Pyruvic acid (Ser) HAMAP MF_00446

Secondary structure

1 ......................... 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56065 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 430A9A537644E4EF

FASTA11712,939
        10         20         30         40         50         60 
MTFEMLYSKI HRATITDANL NYIGSITIDE DLAKLAKLRE GMKVEIVDVN NGERFSTYVI 

        70         80         90        100        110 
LGKKRGEICV NGAAARKVAI GDVVIILAYA SMNEDEINAH KPSIVLVDEK NEILEKG

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.
Nature 388:539-547(1997) [PubMed: 9252185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[2]"Crystal structure of the Schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase."
Lee B.I., Suh S.W.
J. Mol. Biol. 340:1-7(2004) [PubMed: 15184017] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, PROTEOLYTIC PROCESSING BY SELF, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000511 Genomic DNA. Translation: AAD07103.1.
PIRB64524.
RefSeqNP_206836.1. NC_000915.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UHDX-ray2.00A26-117[»]
B1-24[»]
1UHEX-ray1.55A26-117[»]
B1-24[»]
ProteinModelPortalP56065.
SMRP56065. Positions 26-117.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID899139.
GenomeReviewsGene locus HP_0034 in contig AE000511_GR.
KEGGhpy:HP0034.
NMPDRfig|85962.1.peg.34.
PATRIC20591267. VBIHelPyl33062_0035.
TIGRHP_0034.

Phylogenomic databases

HOGENOMHBG302821.
OMALYSKIHR.
ProtClustDBPRK05449.

Family and domain databases

HAMAPMF_00446. PanD.
[Tree]
InterProIPR009010. Asp_de-COase-like_fold.
IPR003190. Asp_decarbox.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
KOK01579.
PANTHERPTHR21012. Asp_decarbox. 1 hit.
PfamPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF006246. Asp_decarbox. 1 hit.
ProDomPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00223. PanD. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAND_HELPY
AccessionPrimary (citable) accession number: P56065
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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