Aspartate 1-decarboxylase precursor - Escherichia coli (strain K12)

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P0A790 (PAND_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase
EC=4.1.1.11

Alternative name(s):
Aspartate alpha-decarboxylase

Gene names

Name:	panD
Ordered Locus Names:	b0131, JW0127

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	126 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Pyruvate Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP protein autoprocessing Inferred from direct assay Ref.5. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 24

Aspartate 1-decarboxylase beta chain HAMAP-Rule MF_00446

PRO_0000023073

Chain

25 – 126

102

Aspartate 1-decarboxylase alpha chain HAMAP-Rule MF_00446

PRO_0000023074

Regions

Region

73 – 75

Substrate binding By similarity

Sites

Active site

Schiff-base intermediate with substrate; via pyruvic acid

Active site

Proton donor

Binding site

Substrate By similarity

Amino acid modifications

Modified residue

Pyruvic acid (Ser) HAMAP-Rule MF_00446

Experimental info

Sequence conflict

107

Y → N Ref.2

Sequence conflict

120 – 121

AI → TV Ref.2

Secondary structure

126

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A790 [UniParc].

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

FASTA

126

13,834

        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' referencesShow '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 277:1453-1474(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.

PIR

C64736.

RefSeq

NP_414673.1. NC_000913.2.
YP_488434.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AW8	X-ray	2.20	A/D	1-24	[»]
			B/E	26-115	[»]
1PPY	X-ray	1.95	A/B	1-126	[»]
1PQE	X-ray	1.95	A	1-126	[»]
1PQF	X-ray	2.00	A/B	1-126	[»]
1PQH	X-ray	1.29	A/B	1-126	[»]
1PT0	X-ray	2.00	A/B	1-126	[»]
1PT1	X-ray	1.90	A/B	1-126	[»]
1PYQ	X-ray	1.90	A/B	1-126	[»]
1PYU	X-ray	1.90	A/C	1-24	[»]
			B/D	26-126	[»]
3TM7	X-ray	1.70	A/C	1-24	[»]
			B/D	25-126	[»]
4AOK	X-ray	1.50	A/D	1-24	[»]
			B/E	26-126	[»]
4AON	X-ray	1.50	A/D	1-24	[»]
			B/E	26-126	[»]
4AZD	X-ray	1.62	A/B	1-126	[»]

ProteinModelPortal

P0A790.

SMR

P0A790. Positions 25-122.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A790. 2 interactions.

STRING

511145.b0131.

Proteomic databases

PRIDE

P0A790.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73242; AAC73242; b0131.
BAB96708; BAB96708; BAB96708.

GeneID

12930736.
945686.

KEGG

ecj:Y75_p0128.
eco:b0131.

PATRIC

32115365. VBIEscCol129921_0134.

Organism-specific databases

EchoBASE

EB1697.

EcoGene

EG11747. panD.

Phylogenomic databases

HOGENOM

HOG000221007.

K01579.

OMA

LYSKIHR.

ProtClustDB

PRK05449.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.

BRENDA

4.1.1.11. 2026.

UniPathway

UPA00028; UER00002.

Gene expression databases

Genevestigator

P0A790.

Family and domain databases

Gene3D

2.40.40.20. 1 hit.

HAMAP

MF_00446. PanD.

InterPro

IPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]

PANTHER

PTHR21012. PTHR21012. 1 hit.

Pfam

PF02261. Asp_decarbox. 1 hit.
[Graphical view]

PIRSF

PIRSF006246. Asp_decarbox. 1 hit.

ProDom

PD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF50692. Asp_decarb_fold. 1 hit.

TIGRFAMs

TIGR00223. panD. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A790.

Entry information

Entry name

PAND_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents