Reviewed, UniProtKB/Swiss-Prot P0A790 (PAND_ECOLI)

Names and origin

Protein names

Recommended name:
    Aspartate 1-decarboxylase
    EC=4.1.1.11
Alternative name(s):
    Aspartate alpha-decarboxylase
Cleaved into 2 chains:
  Recommended name:
      Aspartate 1-decarboxylase beta chain
  Recommended name:
      Aspartate 1-decarboxylase alpha chain

Gene names

Name:	panD
Ordered Locus Names:	b0131, JW0127

Organism

Escherichia coli (strain K12) [Complete 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.
Catalytic activity	L-aspartate = beta-alanine + CO(2).
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.
Pathway	Cofactor biosynthesis; pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subunit structure	Heterooctamer of four alpha and four beta subunits.
Subcellular location	Cytoplasm.
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.
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
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
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

Molecule processing

Chain

1 – 24

24

Aspartate 1-decarboxylase beta chain

Chain

25 – 126

102

Aspartate 1-decarboxylase alpha chain

Regions

Region

73 – 75

3

Substrate binding By similarity

Sites

Active site

25

1

Schiff-base intermediate with substrate; via pyruvic acid

Active site

58

1

Proton donor

Binding site

57

1

Substrate By similarity

Amino acid modifications

Modified residue

25

1

Pyruvic acid (Ser)

Experimental info

Sequence conflict

107

1

Y → N Ref.2

Sequence conflict

120 – 121

2

AI → TV Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

126

Helix Strand Turn

Details...

Beta strand

2 – 14

13

Beta strand

20 – 22

3

Beta strand

26 – 29

4

Helix

30 – 36

7

Beta strand

42 – 48

7

Turn

49 – 51

3

Beta strand

54 – 62

9

Helix

73 – 77

5

Beta strand

84 – 94

11

Helix

95 – 98

4

Beta strand

104 – 109

6

Turn

110 – 112

3

Sequences

	Sequence		Length	Mass (Da)
	P0A790-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: E3169F5C2BDD5D25	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

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: 8837478] [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: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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: 9278503] [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: 16738553] [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: 9169598] [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: 6767707] [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: 12240302] [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: 9546220] [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: 14633979] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS), PROTEOLYTIC PROCESSING BY SELF.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L17086 Genomic DNA. Translation: AAA24274.1.
U00096 Genomic DNA. Translation: AAC73242.1.
AP009048 Genomic DNA. Translation: BAB96708.2.

PIR

C64736.

RefSeq

AP_000792.1.
NP_414673.1.

3D structure databases

PDBMSD

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A790.

Genome annotation databases

GeneID

945686.

GenomeReviews

Gene locus b0131 in contig U00096_GR.
Gene locus JW0127 in contig AP009048_GR.

KEGG

ecj:JW0127.
eco:b0131.

Organism-specific databases

EchoBASE

EB1697.

EcoGene

EG11747. panD.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A790.

Enzyme and pathway databases

BioCyc

EcoCyc:ASPDECARBOX-MON.

Family and domain databases

HAMAP

MF_00446.
[Tree]

InterPro

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

Gene3D

G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.

PANTHER

PTHR21012. Asp_decarbox. 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]

TIGRFAMs

TIGR00223. panD. 1 hit.

BLOCKS

Search...

Other Resources

LinkHub

P0A790.

ProtoNet

Search...

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:	July 22, 2008
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)