Q47NS4 (PAND_THEFY) 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:	Tfu_1862

Organism

Thermobifida fusca (strain YX) [Complete proteome] [HAMAP]

Taxonomic identifier

269800 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida

Protein attributes

Sequence length	137 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. 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_0000236905
	Chain	25 – 137	113	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000236906
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)
	Q47NS4 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 054A245064C0E0D6	FASTA	137	14,524
	10 20 30 40 50 60 MLRTMLNGKI HRATVTHADL HYVGSITIDA DLMDAANLVD GEQVHVVNIT NGHRLVTYVL 70 80 90 100 110 120 TGERGSGVIG INGAAARLVA PGDLVIIISY VQLTEAERAT HRPHVVHVDA NNRIVALGDD 130 LAEPVPGSDQ KSGALLP

References

[1]

"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX." Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N. J. Bacteriol. 189:2477-2486(2007) [PubMed: 17209016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000088 Genomic DNA. Translation: AAZ55895.1.
RefSeq	YP_289918.1. NC_007333.1.
3D structure databases
ProteinModelPortal	Q47NS4.
SMR	Q47NS4. Positions 1-113.
ModBase	Search...
Protein-protein interaction databases
STRING	Q47NS4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3579541.
GenomeReviews	Gene locus Tfu_1862 in contig CP000088_GR.
KEGG	tfu:Tfu_1862.
NMPDR	fig|269800.4.peg.2143.
PATRIC	23904336. VBITheFus33945_2002.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HBG302821.
OMA	LYSKIHR.
PhylomeDB	Q47NS4.
ProtClustDB	PRK05449.
Enzyme and pathway databases
BioCyc	TFUS269800:TFU_1862-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_THEFY

Accession

Primary (citable) accession number: Q47NS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program