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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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)
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

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Pyruvate, 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:SAV2597
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000231591 – 24Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST24
ChainiPRO_000002316025 – 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

Proteomic databases

PaxDbiP65664.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV2597.

Structurei

3D structure databases

ProteinModelPortaliP65664.
SMRiP65664.
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.
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.

P65664-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRTMMNAKI HRARVTESNL NYVGSITIDS DILEAVDILP NEKVAIVNNN
60 70 80 90 100
NGARFETYVI AGERGSGKIC LNGAASRLVE VGDVVIIMTY AQLNEEEIKN
110 120
HAPKVAVMNE DNVIIEMIHE KENTIVL
Length:127
Mass (Da):14,050
Last modified:October 11, 2004 - v1
Checksum:iF3F5BF82DB7C47EA
GO

Sequence cautioni

The sequence BAB58759 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58759.1. Different initiation.
RefSeqiWP_000621532.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58759; BAB58759; SAV2597.
GeneIDi28379769.
KEGGisav:SAV2597.
PATRICi19566130. VBIStaAur52173_2691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB58759.1. Different initiation.
RefSeqiWP_000621532.1. NC_002758.2.

3D structure databases

ProteinModelPortaliP65664.
SMRiP65664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV2597.

Proteomic databases

PaxDbiP65664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB58759; BAB58759; SAV2597.
GeneIDi28379769.
KEGGisav:SAV2597.
PATRICi19566130. VBIStaAur52173_2691.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.

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_STAAM
AccessioniPrimary (citable) accession number: P65664
Secondary accession number(s): Q99R40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 83 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.