F8CWP8 (F8CWP8_GEOTC) 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:	Geoth_1494 EMBL AEH47477.1

Organism

Geobacillus thermoglucosidasius (strain C56-YS93) [Complete proteome] [HAMAP] EMBL AEH47477.1

Taxonomic identifier

634956 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus › Bacillus thermoglucosidasius

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
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)
	F8CWP8 [UniParc]. Last modified September 21, 2011. Version 1. Checksum: 06D32DDEB3F4A161	FASTA	127	14,010
	10 20 30 40 50 60 MFRTLMNAKI HRARVTEANL NYVGSITIDA DILDAVGMVA NEKVQVVNNN NGARFETYII 70 80 90 100 110 120 PGERGSGVFC LNGAAARLVQ KGDIIIVISY AIVPEEKIAQ HRPKIAIMDE NNRIQQLIVE EPAHTVL

References

[1]

"Complete sequence of chromosome of Geobacillus thermoglucosidasius C56-YS93." Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Brumm P. , Kourtz L., Mead D., Woyke T. Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C56-YS93.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002835 Genomic DNA. Translation: AEH47477.1.
RefSeq	YP_004587558.1. NC_015660.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEH47477; AEH47477; Geoth_1494.
GeneID	10787648.
KEGG	gth:Geoth_1494.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K01579.
Enzyme and pathway databases
BioCyc	GTHE634956:GHH3-1627-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

F8CWP8_GEOTC

Accession

Primary (citable) accession number: F8CWP8

Entry history

Integrated into UniProtKB/TrEMBL:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	May 1, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)