B6J1Q5 (B6J1Q5_COXB2) 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
Ordered Locus Names:	CbuG_1590

Organism

Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP] EMBL ACJ18883.1

Taxonomic identifier

434923 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	111 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
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446
Cofactor	Pyruvoyl group By similarity. HAMAP-Rule MF_00446 PIRSR PIRSR006246-1
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity. HAMAP-Rule MF_00446
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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-Rule MF_00446 PIRSR PIRSR006246-3
Sequence similarities	Belongs to the PanD family. HAMAP-Rule MF_00446

Ontologies

Keywords
Biological process	Pantothenate biosynthesis HAMAP-Rule MF_00446
Cellular component	Cytoplasm HAMAP-Rule MF_00446
Ligand	Pyruvate HAMAP-Rule MF_00446 PIRSR PIRSR006246-1 Schiff base HAMAP-Rule MF_00446 PIRSR PIRSR006246-1
Molecular function	Decarboxylase HAMAP-Rule MF_00446 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 HAMAP-Rule MF_00446 PIRSR PIRSR006246-2
Sites
	Active site	25	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-1
	Active site	58	1	Proton donor By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-1
	Binding site	57	1	Substrate By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-2
Amino acid modifications
	Modified residue	25	1	Pyruvic acid (Ser) By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-3

Sequences

	Sequence		Length	Mass (Da)
	B6J1Q5 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 74E7B4CD22DD2ABB	FASTA	111	12,388
	10 20 30 40 50 60 MLISVLKSKI SYATITQKEL FYIGSITIDE AIMERAQLTI NEQVQIVNLN NGERLETYVI 70 80 90 100 110 PGKRNSNIIA LNGPAARKGE IGDQLFILSY ALIDPTQEKL DPVLVDLKLN D

References

[1]

"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella." Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., Samuel J.E., Heinzen R.A. Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CbuG_Q212.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001019 Genomic DNA. Translation: ACJ18883.1.
RefSeq	YP_002304028.1. NC_011527.1.
3D structure databases
ProteinModelPortal	B6J1Q5.
ModBase	Search...
Protein-protein interaction databases
STRING	434923.CbuG_1590. B6J1Q5.
Proteomic databases
PRIDE	B6J1Q5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACJ18883; ACJ18883; CbuG_1590.
GeneID	7014006.
KEGG	cbg:CbuG_1590.
PATRIC	17914261. VBICoxBur10955_1590.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HOG000221007.
KO	K01579.
OMA	LYSKIHR.
ProtClustDB	PRK05449.
Enzyme and pathway databases
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.
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

B6J1Q5_COXB2

Accession

Primary (citable) accession number: B6J1Q5

Entry history

Integrated into UniProtKB/TrEMBL:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)