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UniProtKB - Q72L22 (PAND_THET2)
Protein
Aspartate 1-decarboxylase
Gene
panD
Organism
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Status
Functioni
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
UniRule annotationCatalytic activityi
- EC:4.1.1.11UniRule annotation
Cofactori
pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation
: (R)-pantothenate biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes beta-alanine from L-aspartate.UniRule annotation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 25 | Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation | 1 | |
Binding sitei | 57 | SubstrateUniRule annotation | 1 | |
Active sitei | 58 | Proton donorUniRule annotation | 1 |
GO - Molecular functioni
- aspartate 1-decarboxylase activity Source: UniProtKB-UniRule
GO - Biological processi
- alanine biosynthetic process Source: InterPro
- pantothenate biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Pantothenate biosynthesis |
Ligand | Pyruvate, Schiff base |
Enzyme and pathway databases
UniPathwayi | UPA00028;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:TT_C0241 |
Organismi | Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) |
Taxonomic identifieri | 262724 [NCBI] |
Taxonomic lineagei | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000023181 | 1 – 24 | Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST | 24 | |
ChainiPRO_0000023182 | 25 – 120 | Aspartate 1-decarboxylase alpha chainUniRule annotationAdd BLAST | 96 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 25 | Pyruvic acid (Ser)UniRule annotation | 1 |
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, ZymogenInteractioni
Subunit structurei
Heterooctamer of four alpha and four beta subunits.
UniRule annotationProtein-protein interaction databases
STRINGi | 262724.TT_C0241 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 73 – 75 | Substrate bindingUniRule annotation | 3 |
Sequence similaritiesi
Belongs to the PanD family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0853, Bacteria |
HOGENOMi | CLU_115305_2_0_0 |
OMAi | MLYSKIH |
Family and domain databases
CDDi | cd06919, Asp_decarbox, 1 hit |
HAMAPi | MF_00446, PanD, 1 hit |
InterProi | View protein in InterPro IPR009010, Asp_de-COase-like_dom_sf IPR003190, Asp_decarbox |
PANTHERi | PTHR21012, PTHR21012, 1 hit |
Pfami | View protein in Pfam PF02261, Asp_decarbox, 1 hit |
PIRSFi | PIRSF006246, Asp_decarbox, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit |
TIGRFAMsi | TIGR00223, panD, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q72L22-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKRVMFHAKI HRATVTQADL HYVGSVTVDQ DLLDAAGILP FEQVDIYDIT
60 70 80 90 100
NGARLTTYAL PGERGSGVIG INGAAAHLVK PGDLVILVAY GVFDEEEARN
110 120
LKPTVVLVDE RNRILEVRKG
Sequence cautioni
The sequence AAS80589 differs from that shown. Reason: Erroneous initiation.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE017221 Genomic DNA Translation: AAS80589.1 Different initiation. |
Genome annotation databases
EnsemblBacteriai | AAS80589; AAS80589; TT_C0241 |
KEGGi | tth:TT_C0241 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE017221 Genomic DNA Translation: AAS80589.1 Different initiation. |
3D structure databases
AlphaFoldDBi | Q72L22 |
SMRi | Q72L22 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 262724.TT_C0241 |
Genome annotation databases
EnsemblBacteriai | AAS80589; AAS80589; TT_C0241 |
KEGGi | tth:TT_C0241 |
Phylogenomic databases
eggNOGi | COG0853, Bacteria |
HOGENOMi | CLU_115305_2_0_0 |
OMAi | MLYSKIH |
Enzyme and pathway databases
UniPathwayi | UPA00028;UER00002 |
Family and domain databases
CDDi | cd06919, Asp_decarbox, 1 hit |
HAMAPi | MF_00446, PanD, 1 hit |
InterProi | View protein in InterPro IPR009010, Asp_de-COase-like_dom_sf IPR003190, Asp_decarbox |
PANTHERi | PTHR21012, PTHR21012, 1 hit |
Pfami | View protein in Pfam PF02261, Asp_decarbox, 1 hit |
PIRSFi | PIRSF006246, Asp_decarbox, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit |
TIGRFAMsi | TIGR00223, panD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PAND_THET2 | |
Accessioni | Q72L22Primary (citable) accession number: Q72L22 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 7, 2005 |
Last sequence update: | June 7, 2005 | |
Last modified: | May 25, 2022 | |
This is version 102 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families