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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Binding sitei57 – 571SubstrateUniRule annotation
Active sitei58 – 581Proton donorUniRule annotation

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

BioCyciTTHE300852:GH8R-631-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2424Aspartate 1-decarboxylase beta chainUniRule annotationPRO_0000023183Add
BLAST
Chaini25 – 12096Aspartate 1-decarboxylase alpha chainUniRule annotationPRO_0000023184Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyruvic acid (Ser)UniRule annotation

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

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412Combined sources
Beta strandi17 – 193Combined sources
Beta strandi27 – 293Combined sources
Helixi30 – 367Combined sources
Beta strandi43 – 486Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 585Combined sources
Beta strandi60 – 623Combined sources
Turni64 – 674Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 775Combined sources
Beta strandi84 – 9310Combined sources
Helixi95 – 984Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi114 – 1196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VC3X-ray1.50A1-24[»]
B26-120[»]
2EEOX-ray1.60A1-24[»]
B26-120[»]
ProteinModelPortaliQ5SKN7.
SMRiQ5SKN7. Positions 26-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SKN7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108Z2X. Bacteria.
COG0853. LUCA.
HOGENOMiHOG000221007.
KOiK01579.
OMAiLYSKIHR.
OrthoDBiEOG6P5ZMC.
PhylomeDBiQ5SKN7.

Family and domain databases

HAMAPiMF_00446. PanD.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1VC3X-ray1.50A1-24[»]
B26-120[»]
2EEOX-ray1.60A1-24[»]
B26-120[»]
ProteinModelPortaliQ5SKN7.
SMRiQ5SKN7. Positions 26-120.
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.
OrthoDBiEOG6P5ZMC.
PhylomeDBiQ5SKN7.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.
BioCyciTTHE300852:GH8R-631-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SKN7.

Family and domain databases

HAMAPiMF_00446. PanD.
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...

Publicationsi

  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.

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 11, 2015
This is version 82 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.