Reviewed, UniProtKB/Swiss-Prot Q7NCY1 (PAND1_GLOVI)

Names and origin

Protein names

Recommended name:
    Aspartate 1-decarboxylase 1
    EC=4.1.1.11
Alternative name(s):
    Aspartate alpha-decarboxylase 1
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:	panD1
Ordered Locus Names:	glr2845

Organism

Gloeobacter violaceus [Complete proteome] [HAMAP]

Taxonomic identifier

33072 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Gloeobacteria › Gloeobacterales › Gloeobacter

Protein attributes

Sequence length	118 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_0000023085
	Chain	25 – 118	94	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023086
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)
	Q7NCY1-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: E5C8DA9CBD0699D8	FASTA	118	12,384
	10 20 30 40 50 60 MLRTVLLSKI HRATVTGACL EYMGSISLDA QLLAAAHILA FEQVHVVNLN NGARLITYAI 70 80 90 100 110 EATAGSGAVV LNGAAARLAA PGDRVIVLAY GQGTTEELEN HQPRVVHVDT GNRIVACV

References

[1]

"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids." Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S. DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7421.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000045 Genomic DNA. Translation: BAC90786.1.
RefSeq	NP_925791.1.
3D structure databases
HSSP	HSSP built from PDB template 1PYU based on UniProtKB P31664.
ModBase	Search...
Genome annotation databases
GeneID	2601246.
GenomeReviews	Gene locus glr2845 in contig BA000045_GR.
KEGG	gvi:glr2845.
NMPDR	fig|251221.1.peg.2845.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7NCY1.
OMA	GMISVNG.
Enzyme and pathway databases
BioCyc	GVIO251221:GLR2845-MON.
BRENDA	4.1.1.11. 276183.
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

PAND1_GLOVI

Accession

Primary (citable) accession number: Q7NCY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	December 15, 2003
Last modified:	November 3, 2009
This is version 44 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)