A0Q7L4 (PAND_FRATN) 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:	FTN_1354

Organism

Francisella tularensis subsp. novicida (strain U112) [Complete proteome] [HAMAP]

Taxonomic identifier

401614 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella › Francisella novicida

Protein attributes

Sequence length	111 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-Rule MF_00446
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446
Cofactor	Pyruvoyl group By similarity.
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.
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. HAMAP-Rule 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: 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
Molecule processing
	Chain	1 – 24	24	Aspartate 1-decarboxylase beta chain By similarity		PRO_0000306979
	Chain	25 – 111	87	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000306980
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) HAMAP-Rule MF_00446

Sequences

	Sequence		Length	Mass (Da)
	A0Q7L4 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 22EAAEBC1DB2E5EF	FASTA	111	12,241
	10 20 30 40 50 60 MLISVLKSKI SYATVTGKDL FYVGSITIDS EIMKQANIIE NEKVQVVNLN NGARLETYVI 70 80 90 100 110 KGEPNSKTIA LNGPAARRCE IGDQLFIISY AQVDPTRENI KPKLVDLKTG D

References

[1]

"Comparison of Francisella tularensis genomes reveals evolutionary events associated with the emergence of human pathogenic strains." Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y. , Chang J., Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J. Genome Biol. 8:R102.1-R102.16(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: U112.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000439 Genomic DNA. Translation: ABK90229.1.
RefSeq	YP_898983.1. NC_008601.1.
3D structure databases
ProteinModelPortal	A0Q7L4.
ModBase	Search...
Protein-protein interaction databases
STRING	401614.FTN_1354.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK90229; ABK90229; FTN_1354.
GeneID	4547911.
KEGG	ftn:FTN_1354.
PATRIC	17935865. VBIFraNov128299_1389.
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

PAND_FRATN

Accession

Primary (citable) accession number: A0Q7L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program