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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 catalytic activity are regulated by PanZ in a coenzyme A (CoA)-dependent fashion (PubMed:23170229, PubMed:25910242).3 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

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPantothenate biosynthesis
LigandPyruvate, Schiff base

Enzyme and pathway databases

BioCyciEcoCyc:ASPDECARBOX-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

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 PanZ (PubMed:23170229, PubMed:25910242).3 Publications

Protein-protein interaction databases

BioGridi4259730, 213 interactors
IntActiP0A790, 2 interactors
STRINGi316385.ECDH10B_0111

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 strandi27 – 29Combined sources3
Helixi30 – 36Combined sources7
Beta strandi43 – 48Combined sources6
Turni49 – 51Combined sources3
Beta strandi54 – 58Combined sources5
Beta strandi60 – 62Combined sources3
Beta strandi69 – 72Combined sources4
Helixi73 – 78Combined sources6
Beta strandi84 – 94Combined sources11
Helixi95 – 98Combined sources4
Beta strandi104 – 109Combined sources6
Turni110 – 112Combined sources3
Beta strandi113 – 119Combined sources7

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[»]
5LS7X-ray1.16A1-24[»]
D25-126[»]
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
InterProiView protein in InterPro
IPR009010 Asp_de-COase-like_dom_sf
IPR003190 Asp_decarbox
PANTHERiPTHR21012 PTHR21012, 1 hit
PfamiView protein in Pfam
PF02261 Asp_decarbox, 1 hit
PIRSFiPIRSF006246 Asp_decarbox, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD009294 Asp_decarbox, 1 hit
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
PATRICifig|1411691.4.peg.2151

Similar proteinsi

Entry informationi

Entry nameiPAND_ECOLI
AccessioniPrimary (citable) accession number: P0A790
Secondary accession number(s): P31664, Q8KMY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 28, 2018
This is version 112 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health