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E0UU39 (E0UU39_SULAO) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
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 SAAS SAAS009010

Catalytic activity

L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446 SAAS SAAS009010

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00446 SAAS SAAS009010

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446 SAAS SAAS009010

Subunit structure

Heterooctamer of four alpha and four beta subunits By similarity. HAMAP-Rule MF_00446 SAAS SAAS009010

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00446 SAAS SAAS009010.

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 PIRSR PIRSR006246-3

Sequence similarities

Belongs to the PanD family. HAMAP-Rule MF_00446

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region73 – 753Substrate binding By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-2

Sites

Active site251Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP-Rule MF_00446
Active site581Proton donor By similarity HAMAP-Rule MF_00446
Binding site571Substrate By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-2

Amino acid modifications

Modified residue251Pyruvic acid (Ser) By similarity HAMAP-Rule MF_00446 PIRSR PIRSR006246-3

Sequences

Sequence LengthMass (Da)Tools
E0UU39 [UniParc].

Last modified November 2, 2010. Version 1.
Checksum: CDC69F831D544668

FASTA12113,780
        10         20         30         40         50         60 
MTIEMLYSKI HRATVTDANL NYVGSITIDE ELLEASKMRV GQKVEILNIN NGERFSTYII 

        70         80         90        100        110        120 
LGERGKRDIC LNGAAARKVH KGDKIIVVAY ATYDERELEN YKPRVVLLND ENNIDAIHEE 


I 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002205 Genomic DNA. Translation: ADN08348.1.
RefSeqYP_003891360.1. NC_014506.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN08348; ADN08348; Saut_0299.
GeneID9757815.
KEGGsua:Saut_0299.
PATRIC42440132. VBISulAut92361_0297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221007.
KOK01579.
OMALYSKIHR.

Enzyme and pathway databases

BioCycSAUT563040:GH0V-305-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.
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR00223. panD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameE0UU39_SULAO
AccessionPrimary (citable) accession number: E0UU39
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: February 19, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)