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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.1 Publication

Catalytic activityi

L-aspartate = beta-alanine + CO2.1 Publication

Cofactori

pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

Enzyme regulationi

Inhibited by hydroxylamine, sodium borohydride, D-cycloserine, hydrazine, semicarbazine and succinic dehydrazine (PubMed:6767707). D-serine is a competitive inhibitor (PubMed:6767707). Cleavage and activation of PanD is accelerated by PanM (PubMed:23170229).2 Publications

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes beta-alanine from L-aspartate.
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 acid1
Binding sitei57SubstrateBy similarity1
Active sitei58Proton donor1

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

BioCyciEcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.
BRENDAi4.1.1.11. 2026.
UniPathwayiUPA00028; UER00002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate 1-decarboxylase (EC:4.1.1.11)
Alternative name(s):
Aspartate alpha-decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Name:panD
Ordered Locus Names:b0131, JW0127
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11747. panD.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000230731 – 24Aspartate 1-decarboxylase beta chainAdd BLAST24
ChainiPRO_000002307425 – 126Aspartate 1-decarboxylase alpha chainAdd BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyruvic acid (Ser)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.

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

PaxDbiP0A790.
PRIDEiP0A790.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits (PubMed:9546220). Interacts with PanM (PubMed:23170229).2 Publications

Protein-protein interaction databases

BioGridi4259730. 203 interactors.
IntActiP0A790. 2 interactors.
STRINGi511145.b0131.

Structurei

Secondary structure

1126
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 14Combined sources13
Beta strandi17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Beta strandi26 – 29Combined sources4
Helixi30 – 36Combined sources7
Beta strandi43 – 48Combined sources6
Turni49 – 51Combined sources3
Beta strandi54 – 62Combined sources9
Beta strandi69 – 72Combined sources4
Helixi73 – 77Combined sources5
Beta strandi84 – 94Combined sources11
Helixi95 – 98Combined sources4
Beta strandi104 – 109Combined sources6
Turni110 – 112Combined sources3
Beta strandi113 – 117Combined sources5
Helixi118 – 120Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AW8X-ray2.20A/D1-24[»]
B/E25-115[»]
1PPYX-ray1.95A/B1-126[»]
1PQEX-ray1.95A1-126[»]
1PQFX-ray2.00A/B1-126[»]
1PQHX-ray1.29A/B1-126[»]
1PT0X-ray2.00A/B1-126[»]
1PT1X-ray1.90A/B1-126[»]
1PYQX-ray1.90A/B1-126[»]
1PYUX-ray1.90A/C1-24[»]
B/D25-126[»]
3TM7X-ray1.70A/C1-24[»]
B/D25-126[»]
4AOKX-ray1.50A/D1-24[»]
B/E26-126[»]
4AONX-ray1.50A/D1-24[»]
B/E25-126[»]
4AZDX-ray1.62A/B1-126[»]
4CRYX-ray1.61A1-24[»]
G25-126[»]
4CRZX-ray1.70A1-126[»]
4CS0X-ray2.10A1-126[»]
4D7ZX-ray1.90A1-24[»]
B26-119[»]
ProteinModelPortaliP0A790.
SMRiP0A790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A790.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 75Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the PanD family.Curated

Phylogenomic databases

eggNOGiENOG4108Z2X. Bacteria.
COG0853. LUCA.
HOGENOMiHOG000221007.
InParanoidiP0A790.
KOiK01579.
OMAiLYSKIHR.

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.

P0A790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT
60 70 80 90 100
NGKRFSTYAI AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART
110 120
WRPNVAYFEG DNEMKRTAKA IPVQVA
Length:126
Mass (Da):13,834
Last modified:June 7, 2005 - v1
Checksum:iE3169F5C2BDD5D25
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti107Y → N (PubMed:8202364).Curated1
Sequence conflicti120 – 121AI → TV (PubMed:8202364).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17086 Genomic DNA. Translation: AAA24274.1.
U00096 Genomic DNA. Translation: AAC73242.1.
AP009048 Genomic DNA. Translation: BAB96708.2.
PIRiC64736.
RefSeqiNP_414673.1. NC_000913.3.
WP_000621515.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73242; AAC73242; b0131.
BAB96708; BAB96708; BAB96708.
GeneIDi945686.
KEGGiecj:JW0127.
eco:b0131.
PATRICi32115365. VBIEscCol129921_0134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17086 Genomic DNA. Translation: AAA24274.1.
U00096 Genomic DNA. Translation: AAC73242.1.
AP009048 Genomic DNA. Translation: BAB96708.2.
PIRiC64736.
RefSeqiNP_414673.1. NC_000913.3.
WP_000621515.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AW8X-ray2.20A/D1-24[»]
B/E25-115[»]
1PPYX-ray1.95A/B1-126[»]
1PQEX-ray1.95A1-126[»]
1PQFX-ray2.00A/B1-126[»]
1PQHX-ray1.29A/B1-126[»]
1PT0X-ray2.00A/B1-126[»]
1PT1X-ray1.90A/B1-126[»]
1PYQX-ray1.90A/B1-126[»]
1PYUX-ray1.90A/C1-24[»]
B/D25-126[»]
3TM7X-ray1.70A/C1-24[»]
B/D25-126[»]
4AOKX-ray1.50A/D1-24[»]
B/E26-126[»]
4AONX-ray1.50A/D1-24[»]
B/E25-126[»]
4AZDX-ray1.62A/B1-126[»]
4CRYX-ray1.61A1-24[»]
G25-126[»]
4CRZX-ray1.70A1-126[»]
4CS0X-ray2.10A1-126[»]
4D7ZX-ray1.90A1-24[»]
B26-119[»]
ProteinModelPortaliP0A790.
SMRiP0A790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259730. 203 interactors.
IntActiP0A790. 2 interactors.
STRINGi511145.b0131.

Proteomic databases

PaxDbiP0A790.
PRIDEiP0A790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73242; AAC73242; b0131.
BAB96708; BAB96708; BAB96708.
GeneIDi945686.
KEGGiecj:JW0127.
eco:b0131.
PATRICi32115365. VBIEscCol129921_0134.

Organism-specific databases

EchoBASEiEB1697.
EcoGeneiEG11747. panD.

Phylogenomic databases

eggNOGiENOG4108Z2X. Bacteria.
COG0853. LUCA.
HOGENOMiHOG000221007.
InParanoidiP0A790.
KOiK01579.
OMAiLYSKIHR.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.
BioCyciEcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.
BRENDAi4.1.1.11. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A790.
PROiP0A790.

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_ECOLI
AccessioniPrimary (citable) accession number: P0A790
Secondary accession number(s): P31664, Q8KMY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 105 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.