Reviewed, UniProtKB/Swiss-Prot Q8YR79 (PAND_ANASP)

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:	all3569

Organism

Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	127 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_0000023013
	Chain	25 – 127	103	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023014
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)
	Q8YR79-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 87F768F93C99675D	FASTA	127	14,029
	10 20 30 40 50 60 MQRTLLLAKI HNCTLTGANI NYVGSISIDQ ILLDKSGILP YEQVQVVNNA NGQRFITYAI 70 80 90 100 110 120 PAPAHSGIIE LNGAAARLGI IGDRVIIMTY GQFTSEELKS YTPTVVIVDE KNRPLEVRRY DDLLSQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Soluble inorganic pyrophosphatases from photosynthetic prokaryotes: protein characterization and cloning of ppa genes." Gomez R., Loeffelhardt W., Losada M., Serrano A. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ252206 Genomic DNA. Translation: CAD22577.1. BA000019 Genomic DNA. Translation: BAB75268.1.
PIR	AB2252.
RefSeq	NP_487609.1.
3D structure databases
HSSP	HSSP built from PDB template 1AW8 based on UniProtKB P31664.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8YR79.
Genome annotation databases
GeneID	1107167.
GenomeReviews	Gene locus all3569 in contig BA000019_GR.
KEGG	ana:all3569.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8YR79.
OMA	TTYAIRA.
Enzyme and pathway databases
BioCyc	NSP103690:ALL3569-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_ANASP

Accession

Primary (citable) accession number: Q8YR79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 53 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)