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A4XMZ2 (PAND_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase

EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase
Gene names
Name:panD
Ordered Locus Names:Csac_2708
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP-Rule MF_00446

Catalytic activity

L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00446

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446

Subunit structure

Heterooctamer of four alpha and four beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00446.

Post-translational modification

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 By similarity. HAMAP-Rule MF_00446

Sequence similarities

Belongs to the PanD family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandPyruvate
Schiff base
   Molecular functionDecarboxylase
Lyase
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processalanine biosynthetic process

Inferred from electronic annotation. Source: InterPro

pantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartate 1-decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain By similarity
PRO_1000026165
Chain25 – 128104Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000316056

Regions

Region73 – 753Substrate binding By similarity

Sites

Active site251Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site581Proton donor By similarity
Binding site571Substrate By similarity

Amino acid modifications

Modified residue251Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XMZ2 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E057B70206719CFF

FASTA12814,303
        10         20         30         40         50         60 
MLIEVLKSKI HRATVTEANL NYVGSITIDE ELMEAAGILE NEKVQVVNIN NGERFETYVI 

        70         80         90        100        110        120 
KGERGSGTIC LNGAAARLVQ VGDKVIIMAY CLLTMEEYKT HMPKIVFVDD NNKIVKLSNK 


EEHSECLC 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP68277.1.
RefSeqYP_001181468.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XMZ2.
SMRA4XMZ2. Positions 26-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_2708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP68277; ABP68277; Csac_2708.
GeneID5086714.
KEGGcsc:Csac_2708.
PATRIC21255286. VBICalSac56748_2928.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0853.
HOGENOMHOG000221007.
KOK01579.
OMAWYDGSCA.
OrthoDBEOG6P5ZMC.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-2770-MONOMER.
UniPathwayUPA00028; UER00002.

Family and domain databases

HAMAPMF_00446. PanD.
InterProIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERPTHR21012. PTHR21012. 1 hit.
PfamPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF006246. Asp_decarbox. 1 hit.
ProDomPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR00223. panD. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAND_CALS8
AccessionPrimary (citable) accession number: A4XMZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways