Q2JE00 (PAND1_FRASC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase 1
EC=4.1.1.11

Alternative name(s):
Aspartate alpha-decarboxylase 1

Cleaved into the following 2 chains:

1. Aspartate 1-decarboxylase beta chain
2. Aspartate 1-decarboxylase alpha chain

Gene names

Name:	panD1
Ordered Locus Names:	Francci3_1112

Organism

Frankia sp. (strain CcI3) [Complete proteome] [HAMAP]

Taxonomic identifier

106370 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length	154 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 – 25	25	Aspartate 1-decarboxylase beta chain By similarity		PRO_0000236871
	Chain	26 – 154	129	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000236872
Regions
	Region	74 – 76	3	Substrate binding By similarity
Sites
	Active site	26	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	59	1	Proton donor By similarity
	Binding site	58	1	Substrate By similarity
Amino acid modifications
	Modified residue	26	1	Pyruvic acid (Ser) HAMAP-Rule MF_00446

Sequences

	Sequence		Length	Mass (Da)
	Q2JE00 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 06EAD7B2A79BED6E	FASTA	154	16,409
	10 20 30 40 50 60 MIYREMLKSK IHRAVVRQAD LHYVGSITID ATLMAAAGLW PGEKVDVLDI TNGARLSTYV 70 80 90 100 110 120 IEGEADSGTI GINGAAAHLI SPGDLVIIVG YALMAEEDAR SYQPNVVFVN GDNQLVRMGT 130 140 150 DPAEAYDGVG LVRGDTNSPQ PSLSEQAGDP RRAQ

References

[1]

"Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography." Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., Goltsman E., Huang Y. , Kopp O.R., Labarre L., Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R. Genome Res. 17:7-15(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CcI3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000249 Genomic DNA. Translation: ABD10492.1.
RefSeq	YP_480221.1. NC_007777.1.
3D structure databases
ProteinModelPortal	Q2JE00.
SMR	Q2JE00. Positions 2-114.
ModBase	Search...
Protein-protein interaction databases
STRING	106370.Francci3_1112.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD10492; ABD10492; Francci3_1112.
GeneID	3905454.
KEGG	fra:Francci3_1112.
PATRIC	21925170. VBIFraSp10456_1208.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HOG000221007.
KO	K01579.
OMA	MYDESEM.
Enzyme and pathway databases
BioCyc	FSP106370:GI1F-1182-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.
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

PAND1_FRASC

Accession

Primary (citable) accession number: Q2JE00

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program