D3G0K9 (D3G0K9_BACPE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase HAMAP-Rule MF_00446
EC=4.1.1.11 HAMAP-Rule MF_00446

Alternative name(s):
Aspartate alpha-decarboxylase HAMAP-Rule MF_00446

Gene names

Name:	panD HAMAP-Rule MF_00446 EMBL ADC51171.1
Ordered Locus Names:	BpOF4_15610 EMBL ADC51171.1

Organism

Bacillus pseudofirmus (strain OF4) [Complete proteome] [HAMAP] EMBL ADC51171.1

Taxonomic identifier

398511 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus pseudofirmus

Protein attributes

Sequence length	127 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP-Rule MF_00446 SAAS SAAS003190
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446 SAAS SAAS003190
Cofactor	Pyruvoyl group By similarity. PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446 SAAS SAAS003190
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity. HAMAP-Rule MF_00446 SAAS SAAS003190
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00446 SAAS SAAS003190.
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. PIRSR PIRSR006246-3 HAMAP-Rule MF_00446
Sequence similarities	Belongs to the PanD family. HAMAP-Rule MF_00446

Ontologies

Keywords
Biological process	Pantothenate biosynthesis HAMAP-Rule MF_00446 SAAS SAAS003190
Cellular component	Cytoplasm HAMAP-Rule MF_00446 SAAS SAAS003190
Ligand	Pyruvate PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190 Schiff base PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190
Molecular function	Decarboxylase HAMAP-Rule MF_00446 SAAS SAAS003190 Lyase
PTM	Autocatalytic cleavage HAMAP-Rule MF_00446 Zymogen HAMAP-Rule MF_00446
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	73 – 75	3	Substrate binding By similarity PIRSR PIRSR006246-2 HAMAP-Rule MF_00446
Sites
	Active site	25	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446
	Active site	58	1	Proton donor By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446
	Binding site	57	1	Substrate By similarity PIRSR PIRSR006246-2 HAMAP-Rule MF_00446
Amino acid modifications
	Modified residue	25	1	Pyruvic acid (Ser) By similarity PIRSR PIRSR006246-3 HAMAP-Rule MF_00446

Sequences

	Sequence		Length	Mass (Da)
	D3G0K9 [UniParc]. Last modified March 23, 2010. Version 1. Checksum: 21B92971C85E639A	FASTA	127	14,115
	10 20 30 40 50 60 MYRTMMKAKI HRARVTESNL NYVGSITIDE DIMDAVDILE NEKVQIVNNN NGARFETYVI 70 80 90 100 110 120 KGPRGSKVIC LNGAAARLVQ KDDVVIILSY VMVEESKAAT HTPRVAIMDE TNQIVEMLGT EPASTVM

References

[1]

"Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that support the ability to grow in an external pH range from 7.5 to 11.4." Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J., Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B., Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G. , Xue Y., Ma Y., Hu F.Z., Krulwich T.A. Environ. Microbiol. 13:3289-3309(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OF4 EMBL ADC51171.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001878 Genomic DNA. Translation: ADC51171.1.
RefSeq	YP_003428063.1. NC_013791.2.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADC51171; ADC51171; BpOF4_15610.
GeneID	8768171.
KEGG	bpf:BpOF4_15610.
PATRIC	31948776. VBIBacPse80461_3053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000221007.
KO	K01579.
Enzyme and pathway databases
BioCyc	BPSE398511:GJI9-1592-MONOMER.
UniPathway	UPA00028; UER00002.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
HAMAP	MF_00446. PanD.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR003190. Asp_decarbox. [Graphical view]
PANTHER	PTHR21012. PTHR21012. 1 hit.
Pfam	PF02261. Asp_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF006246. Asp_decarbox. 1 hit.
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR00223. panD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

D3G0K9_BACPE

Accession

Primary (citable) accession number: D3G0K9

Entry history

Integrated into UniProtKB/TrEMBL:	March 23, 2010
Last sequence update:	March 23, 2010
Last modified:	May 1, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)