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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Binding sitei57 – 571SubstrateUniRule annotation
Active sitei58 – 581Proton donorUniRule annotation

GO - Molecular functioni

  1. aspartate 1-decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. alanine biosynthetic process Source: InterPro
  2. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciCSAC351627:GJ17-2770-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:Csac_2708
OrganismiCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
Taxonomic identifieri351627 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
ProteomesiUP000000256 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2424Aspartate 1-decarboxylase beta chainUniRule annotationPRO_1000026165Add
BLAST
Chaini25 – 128104Aspartate 1-decarboxylase alpha chainUniRule annotationPRO_0000316056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyruvic acid (Ser)UniRule annotation

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

STRINGi351627.Csac_2708.

Structurei

3D structure databases

ProteinModelPortaliA4XMZ2.
SMRiA4XMZ2. Positions 26-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanD family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0853.
HOGENOMiHOG000221007.
KOiK01579.
OMAiLYSKIHR.
OrthoDBiEOG6P5ZMC.

Family and domain databases

HAMAPiMF_00446. PanD.
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.

A4XMZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIEVLKSKI HRATVTEANL NYVGSITIDE ELMEAAGILE NEKVQVVNIN
60 70 80 90 100
NGERFETYVI KGERGSGTIC LNGAAARLVQ VGDKVIIMAY CLLTMEEYKT
110 120
HMPKIVFVDD NNKIVKLSNK EEHSECLC
Length:128
Mass (Da):14,303
Last modified:May 29, 2007 - v1
Checksum:iE057B70206719CFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000679 Genomic DNA. Translation: ABP68277.1.
RefSeqiYP_001181468.1. NC_009437.1.

Genome annotation databases

EnsemblBacteriaiABP68277; ABP68277; Csac_2708.
KEGGicsc:Csac_2708.
PATRICi21255286. VBICalSac56748_2928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000679 Genomic DNA. Translation: ABP68277.1.
RefSeqiYP_001181468.1. NC_009437.1.

3D structure databases

ProteinModelPortaliA4XMZ2.
SMRiA4XMZ2. Positions 26-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351627.Csac_2708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP68277; ABP68277; Csac_2708.
KEGGicsc:Csac_2708.
PATRICi21255286. VBICalSac56748_2928.

Phylogenomic databases

eggNOGiCOG0853.
HOGENOMiHOG000221007.
KOiK01579.
OMAiLYSKIHR.
OrthoDBiEOG6P5ZMC.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.
BioCyciCSAC351627:GJ17-2770-MONOMER.

Family and domain databases

HAMAPiMF_00446. PanD.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43494 / DSM 8903.

Entry informationi

Entry nameiPAND_CALS8
AccessioniPrimary (citable) accession number: A4XMZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: April 1, 2015
This is version 51 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.