Reviewed, UniProtKB/Swiss-Prot Q7WHJ6 (PAND_BORBR)

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- Recommended name:
            Aspartate 1-decarboxylase beta chain
    2- Recommended name:
            Aspartate 1-decarboxylase alpha chain

Gene names

Name:	panD
Ordered Locus Names:	BB3211

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity.
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446
Cofactor	Pyruvoyl group By similarity.
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.
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.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: HAMAP 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_0000023041
	Chain	25 – 122	98	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023042
Regions
	Region	73 – 75	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) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WHJ6-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 17AEE76FA2EB2C3E	FASTA	122	13,579
	10 20 30 40 50 60 MQRIMLRAKL HRVTVTEADL HYEGSCGIDE DLLDAAGMRE FERIELYNVT NGERFDTYII 70 80 90 100 110 120 KAARGSGAIS LNGAAARRAQ VGDLLIICTY GPMSEEQSAT HKPQVVLVDD ANRVKEIRKF PA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640446 Genomic DNA. Translation: CAE33703.1.
RefSeq	NP_889747.1.
3D structure databases
HSSP	HSSP built from PDB template 1PYU based on UniProtKB P31664.
ModBase	Search...
Genome annotation databases
GeneID	2661273.
GenomeReviews	Gene locus BB3211 in contig BX470250_GR.
KEGG	bbr:BB3211.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WHJ6.
OMA	TTYAIRA.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3211-MON.
BRENDA	4.1.1.11. 413.
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.
ProtoNet	Search...

Entry information

Entry name

PAND_BORBR

Accession

Primary (citable) accession number: Q7WHJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 41 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)