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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Bacillus anthracis
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), Aspartate 1-decarboxylase (panD), Aspartate 1-decarboxylase (panD), 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:BA_1564, GBAA_1564, BAS1451
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000000427 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000230171 – 24Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST24
ChainiPRO_000002301825 – 127Aspartate 1-decarboxylase alpha chainUniRule annotationAdd BLAST103

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

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi260799.BAS1451

Structurei

3D structure databases

ProteinModelPortaliQ81ST1
SMRiQ81ST1
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.

Q81ST1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRTMMRAKL HRATVTEANL NYVGSITIDE DLMDAVNIVE NEKVQIVNNN
60 70 80 90 100
NGARLETYVI KGERGSGVVC LNGAAARLVQ PGDKVIIICY GLVAEENIHK
110 120
QEPKIAVLDD DNQIIEMLGA EKAGTIL
Length:127
Mass (Da):13,909
Last modified:June 1, 2003 - v1
Checksum:i62AE66D682F1453B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA Translation: AAP25500.1
AE017334 Genomic DNA Translation: AAT30661.1
AE017225 Genomic DNA Translation: AAT53771.1
RefSeqiNP_844014.1, NC_003997.3
WP_000490176.1, NZ_NVHS01000045.1
YP_027720.1, NC_005945.1

Genome annotation databases

EnsemblBacteriaiAAP25500; AAP25500; BA_1564
AAT30661; AAT30661; GBAA_1564
AAT53771; AAT53771; BAS1451
GeneIDi1086955
2850816
29402314
KEGGiban:BA_1564
bar:GBAA_1564
bat:BAS1451
PATRICifig|198094.11.peg.1534

Similar proteinsi

Entry informationi

Entry nameiPAND_BACAN
AccessioniPrimary (citable) accession number: Q81ST1
Secondary accession number(s): Q6I111, Q6KUW5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2003
Last modified: April 25, 2018
This is version 106 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