Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

BioCyciFTUL177416:G1G1C-1587-MONOMER
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:FTT_1391
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003069811 – 24Aspartate 1-decarboxylase beta chainUniRule annotationAdd BLAST24
ChainiPRO_000030698225 – 111Aspartate 1-decarboxylase alpha chainUniRule annotationAdd BLAST87

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

STRINGi177416.FTT_1391

Structurei

Secondary structure

1111
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 14Combined sources13
Beta strandi17 – 21Combined sources5
Beta strandi26 – 29Combined sources4
Helixi30 – 35Combined sources6
Beta strandi42 – 48Combined sources7
Turni49 – 51Combined sources3
Beta strandi54 – 62Combined sources9
Beta strandi69 – 72Combined sources4
Helixi73 – 78Combined sources6
Beta strandi84 – 93Combined sources10
Beta strandi103 – 106Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OUGX-ray1.55A/B/C/E/F/G/H/I1-111[»]
ProteinModelPortaliQ5NF56
SMRiQ5NF56
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5NF56

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.

Q5NF56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLISVLKSKI SYATVTGKDL FYVGSITIDS EIMKQANIIE NEKVQVVNLN
60 70 80 90 100
NGERLETYVI KGEPNSKTIA LNGPAARRCE IGDQLFIISY TQVDPTRENI
110
KPKLVDLKTG D
Length:111
Mass (Da):12,329
Last modified:February 1, 2005 - v1
Checksum:i22EAAAB806B751EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA Translation: CAG46024.1
RefSeqiWP_003022192.1, NZ_CP010290.1
YP_170336.1, NC_006570.2

Genome annotation databases

EnsemblBacteriaiCAG46024; CAG46024; FTT_1391
GeneIDi3191388
KEGGiftu:FTT_1391

Similar proteinsi

Entry informationi

Entry nameiPAND_FRATT
AccessioniPrimary (citable) accession number: Q5NF56
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 1, 2005
Last modified: May 23, 2018
This is version 81 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, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health