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P0A790 (PAND_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase

EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase
Gene names
Name:panD
Ordered Locus Names:b0131, JW0127
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length126 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. Ref.6

Catalytic activity

L-aspartate = beta-alanine + CO2. Ref.6

Cofactor

Pyruvoyl group.

Enzyme regulation

Inhibited by hydroxylamine, phenylhydrazine, sodium borohydride, D-cycloserine, hydrazine, semicarbazine and succinic dehydrazine. L-glutamate, succinate, oxaloacetate, L-serine, L-cysteic acid, beta-hydroxy-DL-asparate, and D-serine are competitive inhibitors By similarity. Ref.6

Pathway

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

Subunit structure

Heterooctamer of four alpha and four beta subunits. Ref.8

Subcellular location

Cytoplasm Ref.6.

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-Rule MF_00446

Sequence similarities

Belongs to the PanD family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain HAMAP-Rule MF_00446
PRO_0000023073
Chain25 – 126102Aspartate 1-decarboxylase alpha chain HAMAP-Rule MF_00446
PRO_0000023074

Regions

Region73 – 753Substrate binding By similarity

Sites

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

Amino acid modifications

Modified residue251Pyruvic acid (Ser) HAMAP-Rule MF_00446

Experimental info

Sequence conflict1071Y → N Ref.2
Sequence conflict120 – 1212AI → TV Ref.2

Secondary structure

......................... 126
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A790 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: E3169F5C2BDD5D25

FASTA12613,834
        10         20         30         40         50         60 
MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT NGKRFSTYAI 

        70         80         90        100        110        120 
AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART WRPNVAYFEG DNEMKRTAKA 


IPVQVA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and sequence of the Escherichia coli panBCD gene cluster."
Merkel W.K., Nichols B.P.
FEMS Microbiol. Lett. 143:247-252(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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], SEQUENCE REVISION TO 107 AND 120-121.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry."
Ramjee M.K., Genschel U., Abell C., Smith A.G.
Biochem. J. 323:661-669(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5 AND 25-29, CHARACTERIZATION.
[6]"Beta-alanine synthesis in Escherichia coli."
Cronan J.E. Jr.
J. Bacteriol. 141:1291-1297(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[7]"Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction."
Saldanha S.A., Birch L.M., Webb M.E., Nabbs B.K., von Delft F., Smith A.G., Abell C.
Chem. Commun. (Camb.) 18:1760-1761(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME MECHANISM.
[8]"Crystal structure of aspartate decarboxylase at 2.2-A resolution provides evidence for an ester in protein self-processing."
Albert A., Dhanaraj V., Genschel U., Khan G., Ramjee M.K., Pulido R., Sibanda B.L., von Delft F., Witty M., Blundell T.L., Smith A.G., Abell C.
Nat. Struct. Biol. 5:289-293(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-115, PROTEOLYTIC PROCESSING BY SELF, SUBUNIT.
[9]"Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase."
Schmitzberger F., Kilkenny M.L., Lobley C.M.C., Webb M.E., Vinkovic M., Matak-Vinkovic D., Witty M., Chirgadze D.Y., Smith A.G., Abell C., Blundell T.L.
EMBO J. 22:6193-6204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS), PROTEOLYTIC PROCESSING BY SELF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L17086 Genomic DNA. Translation: AAA24274.1.
U00096 Genomic DNA. Translation: AAC73242.1.
AP009048 Genomic DNA. Translation: BAB96708.2.
PIRC64736.
RefSeqNP_414673.1. NC_000913.3.
YP_488434.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW8X-ray2.20A/D1-24[»]
B/E26-115[»]
1PPYX-ray1.95A/B1-126[»]
1PQEX-ray1.95A1-126[»]
1PQFX-ray2.00A/B1-126[»]
1PQHX-ray1.29A/B1-126[»]
1PT0X-ray2.00A/B1-126[»]
1PT1X-ray1.90A/B1-126[»]
1PYQX-ray1.90A/B1-126[»]
1PYUX-ray1.90A/C1-24[»]
B/D26-126[»]
3TM7X-ray1.70A/C1-24[»]
B/D25-126[»]
4AOKX-ray1.50A/D1-24[»]
B/E26-126[»]
4AONX-ray1.50A/D1-24[»]
B/E26-126[»]
4AZDX-ray1.62A/B1-126[»]
ProteinModelPortalP0A790.
SMRP0A790. Positions 25-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A790. 2 interactions.
STRING511145.b0131.

Proteomic databases

PRIDEP0A790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73242; AAC73242; b0131.
BAB96708; BAB96708; BAB96708.
GeneID12930736.
945686.
KEGGecj:Y75_p0128.
eco:b0131.
PATRIC32115365. VBIEscCol129921_0134.

Organism-specific databases

EchoBASEEB1697.
EcoGeneEG11747. panD.

Phylogenomic databases

HOGENOMHOG000221007.
KOK01579.
OMALYSKIHR.
OrthoDBEOG6P5ZMC.
ProtClustDBPRK05449.

Enzyme and pathway databases

BioCycEcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.
BRENDA4.1.1.11. 2026.
UniPathwayUPA00028; UER00002.

Gene expression databases

GenevestigatorP0A790.

Family and domain databases

HAMAPMF_00446. PanD.
InterProIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERPTHR21012. PTHR21012. 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. SSF50692. 1 hit.
TIGRFAMsTIGR00223. panD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A790.
PROP0A790.

Entry information

Entry namePAND_ECOLI
AccessionPrimary (citable) accession number: P0A790
Secondary accession number(s): P31664, Q8KMY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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