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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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), 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

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPantothenate biosynthesis
LigandPyruvate, 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:SF0128, S0130
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB02175 Malonic acid
DB03382 S-Oxy Cysteine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000231551 – 24Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST24
ChainiPRO_000002315625 – 126Aspartate 1-decarboxylase alpha chainUniRule annotationAdd BLAST102

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

Proteomic databases

PRIDEiP0A793

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP0A793
SMRiP0A793
ModBaseiSearch...
MobiDBiSearch...

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

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.

P0A793-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA Translation: AAN41791.2
AE014073 Genomic DNA Translation: AAP15672.1
RefSeqiNP_706084.2, NC_004337.2
WP_000621515.1, NZ_NIYV01000058.1

Genome annotation databases

EnsemblBacteriaiAAN41791; AAN41791; SF0128
AAP15672; AAP15672; S0130
GeneIDi1024489
KEGGisfl:SF0128
sfx:S0130
PATRICifig|198214.7.peg.144

Similar proteinsi

Entry informationi

Entry nameiPAND_SHIFL
AccessioniPrimary (citable) accession number: P0A793
Secondary accession number(s): P31664, Q8KMY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 25, 2018
This is version 90 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health