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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Porticoccaceae bacterium
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.UniRule annotationSAAS annotation

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-aspartate = beta-alanine + CO2.UniRule annotationSAAS 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 annotationSAAS 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), 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 functionDecarboxylaseUniRule annotationSAAS annotation, Lyase
Biological processPantothenate biosynthesisUniRule annotationSAAS annotation
LigandPyruvateUniRule annotationSAAS annotation, Schiff baseUniRule annotationSAAS annotation

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 alpha chainUniRule annotation
Aspartate 1-decarboxylase beta chainUniRule annotation
Gene namesi
Name:panDUniRule annotation
ORF Names:CMK36_03235Imported
OrganismiPorticoccaceae bacteriumImported
Taxonomic identifieri2026782 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesPorticoccaceae
Proteomesi
  • UP000231033 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_50140057561 – 24Aspartate 1-decarboxylaseUniRule annotationAdd BLAST24
ChainiPRO_501400575525 – 118Aspartate 1-decarboxylaseUniRule annotationAdd BLAST94

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 cleavageUniRule annotation, ZymogenUniRule annotation

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotationSAAS annotation

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 75Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the PanD family.UniRule annotationSAAS annotation

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.

A0A2E9XJP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLTFLKSKL HMASVTGAEL MYDGSCAIDA NLLAAAKMSE FEQIDIYNVT
60 70 80 90 100
NGKRFTTYII CARAGSGIIS MNGAAARKCQ IGDRIIIATY ASYDGAATAH
110
RPRLVYLRSD NSIERQDG
Length:118
Mass (Da):12,830
Last modified:January 31, 2018 - v1
Checksum:i1CCBEF03565B7D15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
PCCK01000024 Genomic DNA Translation: MBV32439.1

Similar proteinsi

Entry informationi

Entry nameiA0A2E9XJP2_9GAMM
AccessioniPrimary (citable) accession number: A0A2E9XJP2
Entry historyiIntegrated into UniProtKB/TrEMBL: January 31, 2018
Last sequence update: January 31, 2018
Last modified: May 23, 2018
This is version 5 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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