Q8FU86 (PAND_COREF) 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:	CE0135

Organism

Corynebacterium efficiens [Complete proteome] [HAMAP]

Taxonomic identifier

152794 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00446
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity.
Subcellular location	Cytoplasm By similarity HAMAP 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 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: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
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_0000023065
	Chain	25 – 136	112	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023066
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) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FU86 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 9C5042CB497CCC3D	FASTA	136	14,098
	10 20 30 40 50 60 MLRTILGSKI HRATVTQADL DYVGSITIDA DLVNAAGLIE GEKVAVVDIT NGARIETYVI 70 80 90 100 110 120 TGDAGTGSIC INGAAAHLIN PGDLVIIMSY LQATDAEARA YQPNIVHVDA DNRIVALGND 130 AGEPIPGSSL LSSRSL

References

[1]

"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000035 Genomic DNA. Translation: BAC16945.1.
RefSeq	NP_736745.1. NC_004369.1.
3D structure databases
ProteinModelPortal	Q8FU86.
SMR	Q8FU86. Positions 1-113.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1031997.
GenomeReviews	Gene locus CE0135 in contig BA000035_GR.
KEGG	cef:CE0135.
NMPDR	fig|196164.1.peg.135.
PATRIC	21486458. VBICorEff9312_0183.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG302821.
OMA	LYSKIHR.
PhylomeDB	Q8FU86.
ProtClustDB	PRK05449.
Enzyme and pathway databases
BioCyc	CEFF196164:CE0135-MONOMER.
Family and domain databases
HAMAP	MF_00446. PanD. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR003190. Asp_decarbox. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
KO	K01579.
PANTHER	PTHR21012. Asp_decarbox. 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_COREF

Accession

Primary (citable) accession number: Q8FU86

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program