Reviewed, UniProtKB/Swiss-Prot A0RM41 (PAND_CAMFF)

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:	CFF8240_0064

Organism

Campylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]

Taxonomic identifier

360106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	115 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.
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_0000306945
	Chain	25 – 115	91	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000306946
Regions
	Region	72 – 74	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)
	A0RM41-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: F89E12611BACF2FA	FASTA	115	13,017
	10 20 30 40 50 60 MEIEMLYSKI HRATVTDANL NYVGSITIDE RLMKAANLLE FQKVEILDIN NGERFQTYVI 70 80 90 100 110 KGEKKGEICL NGAAARKVCI GDIIIIVSYA SMKRKKAKNF SPTIVHVNEK NEINE

References

[1]	"Sequence of Campylobacter fetus subsp. fetus 82-40." Fouts D.E., Nelson K.E. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000487 Genomic DNA. Translation: ABK82082.1.
RefSeq	YP_891274.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0RM41.
Genome annotation databases
GeneID	4538981.
GenomeReviews	Gene locus CFF8240_0064 in contig CP000487_GR.
KEGG	cff:CFF8240_0064.
NMPDR	fig|360106.5.peg.63.
TIGR	CFF8240_0064.
Phylogenomic databases
OMA	TTYAIRA.
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_CAMFF

Accession

Primary (citable) accession number: A0RM41

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	January 9, 2007
Last modified:	November 3, 2009
This is version 21 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)