A8FEH5 (PAND_BACP2) 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:	BPUM_1972

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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. 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_1000060266
	Chain	25 – 127	103	Aspartate 1-decarboxylase alpha chain By similarity		PRO_1000060267
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)
	A8FEH5 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: D53788994A2B1441	FASTA	127	13,920
	10 20 30 40 50 60 MYRTFMTSKL HKATVTEANL HYVGSITIDE DLLDAAGMMA NEKVQIVNNH NGARLETYII 70 80 90 100 110 120 PGERKSGVIC LNGAAARLVQ PGDEVIIIAY GMLSEGEAKT HTPKVVVLNK ENQIEQMIGQ EPARTIL

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV62642.1.
RefSeq	YP_001487202.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FEH5.
SMR	A8FEH5. Positions 26-117.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FEH5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000066154; EBBACP00000064487; EBBACG00000066145.
GeneID	5621241.
GenomeReviews	Gene locus BPUM_1972 in contig CP000813_GR.
KEGG	bpu:BPUM_1972.
PATRIC	18967844. VBIBacPum16546_2018.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
GeneTree	EBGT00050000002424.
HOGENOM	HBG302821.
OMA	LYSKIHR.
ProtClustDB	PRK05449.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_1972-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_BACP2

Accession

Primary (citable) accession number: A8FEH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program