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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.UniRule annotation

Catalytic activityi

L-aspartate = beta-alanine + CO2.UniRule annotation

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes beta-alanine from L-aspartate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Aspartate 1-decarboxylase (panD)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes beta-alanine from L-aspartate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei25Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation1
Binding sitei57SubstrateUniRule annotation1
Active sitei58Proton donorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate 1-decarboxylaseUniRule annotation (EC:4.1.1.11UniRule annotation)
Alternative name(s):
Aspartate alpha-decarboxylaseUniRule annotation
Cleaved into the following 2 chains:
Aspartate 1-decarboxylase beta chainUniRule annotation
Aspartate 1-decarboxylase alpha chainUniRule annotation
Gene namesi
Name:panDUniRule annotation
Ordered Locus Names:TTHA0606
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000231831 – 24Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST24
ChainiPRO_000002318425 – 120Aspartate 1-decarboxylase alpha chainUniRule annotationAdd BLAST96

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyruvic acid (Ser)UniRule annotation1

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA0606.

Structurei

Secondary structure

1120
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 14Combined sources12
Beta strandi17 – 19Combined sources3
Beta strandi27 – 29Combined sources3
Helixi30 – 36Combined sources7
Beta strandi43 – 48Combined sources6
Turni49 – 51Combined sources3
Beta strandi54 – 58Combined sources5
Beta strandi60 – 62Combined sources3
Turni64 – 67Combined sources4
Beta strandi69 – 72Combined sources4
Helixi73 – 77Combined sources5
Beta strandi84 – 93Combined sources10
Helixi95 – 98Combined sources4
Beta strandi104 – 108Combined sources5
Beta strandi114 – 119Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VC3X-ray1.50A1-24[»]
B26-120[»]
2EEOX-ray1.60A1-24[»]
B26-120[»]
ProteinModelPortaliQ5SKN7.
SMRiQ5SKN7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SKN7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 75Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the PanD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108Z2X. Bacteria.
COG0853. LUCA.
HOGENOMiHOG000221007.
KOiK01579.
OMAiLYSKIHR.
PhylomeDBiQ5SKN7.

Family and domain databases

CDDicd06919. Asp_decarbox. 1 hit.
HAMAPiMF_00446. PanD. 1 hit.
InterProiIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERiPTHR21012. PTHR21012. 1 hit.
PfamiPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF006246. Asp_decarbox. 1 hit.
ProDomiPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR00223. panD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5SKN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRVMFHAKI HRATVTQADL HYVGSVTVDQ DLLDAAGILP FEQVDIYDIT
60 70 80 90 100
NGARLTTYAL PGERGSGVIG INGAAAHLVK PGDLVILVAY GVFDEEEARN
110 120
LKPTVVLVDE RNRILEVRKG
Length:120
Mass (Da):13,095
Last modified:December 21, 2004 - v1
Checksum:iBAD37D3B6DDD1304
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70429.1.
RefSeqiWP_011228064.1. NC_006461.1.
YP_143872.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70429; BAD70429; BAD70429.
GeneIDi3169478.
KEGGittj:TTHA0606.
PATRICi23956187. VBITheThe93045_0604.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70429.1.
RefSeqiWP_011228064.1. NC_006461.1.
YP_143872.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VC3X-ray1.50A1-24[»]
B26-120[»]
2EEOX-ray1.60A1-24[»]
B26-120[»]
ProteinModelPortaliQ5SKN7.
SMRiQ5SKN7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0606.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70429; BAD70429; BAD70429.
GeneIDi3169478.
KEGGittj:TTHA0606.
PATRICi23956187. VBITheThe93045_0604.

Phylogenomic databases

eggNOGiENOG4108Z2X. Bacteria.
COG0853. LUCA.
HOGENOMiHOG000221007.
KOiK01579.
OMAiLYSKIHR.
PhylomeDBiQ5SKN7.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.

Miscellaneous databases

EvolutionaryTraceiQ5SKN7.

Family and domain databases

CDDicd06919. Asp_decarbox. 1 hit.
HAMAPiMF_00446. PanD. 1 hit.
InterProiIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERiPTHR21012. PTHR21012. 1 hit.
PfamiPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF006246. Asp_decarbox. 1 hit.
ProDomiPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR00223. panD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAND_THET8
AccessioniPrimary (citable) accession number: Q5SKN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.