Q5SKN7 (PAND_THET8) 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:	TTHA0606

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	120 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	3D-structure Complete proteome Reference 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_0000023183

Chain

25 – 120

96

Aspartate 1-decarboxylase alpha chain By similarity

PRO_0000023184

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

Secondary structure

1

.

.

.

.

.

120

Helix Strand Turn

Details...

Beta strand

2 – 14

13

Beta strand

17 – 19

3

Sequences

	Sequence		Length	Mass (Da)
	Q5SKN7 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: BAD37D3B6DDD1304	FASTA	120	13,095
	10 20 30 40 50 60 MKRVMFHAKI HRATVTQADL HYVGSVTVDQ DLLDAAGILP FEQVDIYDIT NGARLTTYAL 70 80 90 100 110 120 PGERGSGVIG INGAAAHLVK PGDLVILVAY GVFDEEEARN LKPTVVLVDE RNRILEVRKG

References

[1]

"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD70429.1.

RefSeq

YP_143872.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VC3	X-ray	1.50	A	1-24	[»]
			B	26-120	[»]
2EEO	X-ray	1.60	A	1-24	[»]
			B	26-120	[»]

ProteinModelPortal

Q5SKN7.

SMR

Q5SKN7. Positions 26-120.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA0606.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD70429; BAD70429; BAD70429.

GeneID

3169478.

KEGG

ttj:TTHA0606.

PATRIC

23956187. VBITheThe93045_0604.

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...

Other

EvolutionaryTrace

Q5SKN7.

Entry information

Entry name

PAND_THET8

Accession

Primary (citable) accession number: Q5SKN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program