Reviewed, UniProtKB/Swiss-Prot Q2T096 (PAND_BURTA)

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:	BTH_I0847

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	128 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_0000236857
	Chain	25 – 128	104	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000236858
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)
	Q2T096-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 8CD6E1C390F899BC	FASTA	128	14,349
	10 20 30 40 50 60 MQRHMLKSKI HRAAVTHCEL HYEGSCAIDE DLLEAANIVE NERIDIWNIN NGERFSTYAI 70 80 90 100 110 120 KGERGSGMIS LNGSAARRAQ LGDLVIIAAF AMIDEEELKA GWKPDLVFVD EGNKIKGSRD HVPTQNWT

References

[1]

Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000086 Genomic DNA. Translation: ABC38409.1.
RefSeq	YP_441403.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2T096.
Genome annotation databases
GeneID	3848384.
GenomeReviews	Gene locus BTH_I0847 in contig CP000086_GR.
KEGG	bte:BTH_I0847.
TIGR	BTH_I0847.
Phylogenomic databases
HOGENOM	Q2T096.
OMA	TTYAIRA.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_I0847-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.
ProtoNet	Search...

Entry information

Entry name

PAND_BURTA

Accession

Primary (citable) accession number: Q2T096

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	January 24, 2006
Last modified:	November 3, 2009
This is version 28 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)