Q18HQ3 (PAND_HALWD) 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:	HQ2363A

Organism

Haloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]

Taxonomic identifier

362976 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloquadratum

Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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_0000307089
	Chain	25 – 114	90	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000307090
Regions
	Region	71 – 73	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) HAMAP MF_00446

Sequences

	Sequence		Length	Mass (Da)
	Q18HQ3 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 70BA7AB3BCEAA79F	FASTA	114	12,796
	10 20 30 40 50 60 MRRWLLKSKL HRARVTGTEK DYEGSISIDA ALLSEADIAV GEQVQVVNVT NGERFETYTI 70 80 90 100 110 EGESRQMELN GAAARLAETG DVIIVISYGL YVKDEQPEPT VLLLDEENRI SERE

References

[1]

"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity." Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D. BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 16790.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180088 Genomic DNA. Translation: CAJ52484.1.
RefSeq	YP_658098.1. NC_008212.1.
3D structure databases
ProteinModelPortal	Q18HQ3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q18HQ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4194405.
GenomeReviews	Gene locus HQ2363A in contig AM180088_GR.
KEGG	hwa:HQ2363A.
NMPDR	fig|362976.6.peg.1375.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG17337.
HOGENOM	HBG302821.
OMA	GSREINL.
PhylomeDB	Q18HQ3.
Enzyme and pathway databases
BioCyc	HWAL362976:HQ2363A-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_HALWD

Accession

Primary (citable) accession number: Q18HQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	July 25, 2006
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program