Q29W39 (PAND_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	CJJ81176_0319

Organism

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]

Taxonomic identifier

354242 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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 By similarity. HAMAP MF_00446
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00446
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 By similarity.
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 By similarity. HAMAP 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	Complete proteome
Gene Ontology (GO)
Biological process	alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 24	24	Aspartate 1-decarboxylase beta chain By similarity		PRO_0000306947
	Chain	25 – 126	102	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000306948
Regions
	Region	72 – 74	3	Substrate binding By similarity
Sites
	Active site	25	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	58	1	Proton donor By similarity
	Binding site	57	1	Substrate By similarity
Amino acid modifications
	Modified residue	25	1	Pyruvic acid (Ser) HAMAP MF_00446

Sequences

	Sequence		Length	Mass (Da)
	Q29W39 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 75DDF20D43EEF12E	FASTA	126	13,987
	10 20 30 40 50 60 MNITLLKSKI HRANVTEARL DYVGSISIDE KLLQASGILE YEKVQVVNVN NGARFETYTI 70 80 90 100 110 120 ATQEEGVVCL NGAAARLAEV GDKVIIMSYA DFNEEEAKTF KPKVVFVDEN NTATKITNYE KHGAIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Global expression profiling of the flagella regulon of Campylobacter jejuni 81-176 reveals a novel virulence determinant." Goon S.C., Holder L., Majam G., Lorenzo M., Pattarini D., Ewing C.P., Batchelor R., Guerry P. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Fouts D.E., Nelson K.E., Sebastian Y. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 81-176.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY923838 Genomic DNA. Translation: AAX99086.1. CP000538 Genomic DNA. Translation: EAQ73317.1.
RefSeq	YP_001000007.1. NC_008787.1.
3D structure databases
ProteinModelPortal	Q29W39.
ModBase	Search...
Protein-protein interaction databases
STRING	Q29W39.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4683745.
GenomeReviews	Gene locus CJJ81176_0319 in contig CP000538_GR.
KEGG	cjj:CJJ81176_0319.
PATRIC	20050594. VBICamJej103413_0340.
TIGR	CJJ81176_0319.
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HBG302821.
OMA	LYSKIHR.
PhylomeDB	Q29W39.
ProtClustDB	PRK05449.
Enzyme and pathway databases
BioCyc	CJEJ354242:CJJ81176_0319-MONOMER.
Family and domain databases
HAMAP	MF_00446. PanD. [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.
KO	K01579.
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]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR00223. PanD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAND_CAMJJ

Accession

Primary (citable) accession number: Q29W39

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	April 4, 2006
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program