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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Unreviewed-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 annotationSAAS annotation

Catalytic activityi

L-aspartate = beta-alanine + CO2.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation
  • pyruvoyl groupUniRule annotationSAAS 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

DecarboxylaseUniRule annotationSAAS annotation, Lyase

Keywords - Biological processi

Pantothenate biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

PyruvateUniRule annotation, Schiff baseUniRule annotation

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-138-MONOMER.
UniPathwayiUPA00028; UER00002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate 1-decarboxylaseUniRule annotationSAAS annotation (EC:4.1.1.11UniRule annotationSAAS annotation)
Alternative name(s):
Aspartate alpha-decarboxylaseUniRule annotation
Gene namesi
Name:panDUniRule annotationImported
ORF Names:HMPREF0290_2595Imported
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)Imported
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

PTM / Processingi

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 cleavageUniRule annotation, ZymogenUniRule annotation

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliC8NRH0.
SMRiC8NRH0. Positions 1-113.
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.
KOiK01579.
OMAiYEMVQIS.

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.

C8NRH0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRTILGSKI HRATVTQADL DYVGSITIDA DLVNAAGLIE GEKVAVVDIT
60 70 80 90 100
NGARIETYVI TGDAGTGSIC INGAAAHLIN PGDLVIIMSY LQATDAEARA
110 120 130
YQPNIVHVDA DNRIVALGND AGEPIPGSSL LSSRSL
Length:136
Mass (Da):14,098
Last modified:November 3, 2009 - v1
Checksum:i9C5042CB497CCC3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACLI01000106 Genomic DNA. Translation: EEW48818.1.
RefSeqiNP_736745.1. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiEEW48818; EEW48818; HMPREF0290_2595.
GeneIDi1031997.
KEGGicef:CE0135.
PATRICi21486458. VBICorEff9312_0183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACLI01000106 Genomic DNA. Translation: EEW48818.1.
RefSeqiNP_736745.1. NC_004369.1.

3D structure databases

ProteinModelPortaliC8NRH0.
SMRiC8NRH0. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEEW48818; EEW48818; HMPREF0290_2595.
GeneIDi1031997.
KEGGicef:CE0135.
PATRICi21486458. VBICorEff9312_0183.

Phylogenomic databases

eggNOGiCOG0853.
KOiK01579.
OMAiYEMVQIS.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00002.
BioCyciCEFF196164:GJW8-138-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. Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.
    , Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.
    Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: YS-314Imported.

Entry informationi

Entry nameiC8NRH0_COREF
AccessioniPrimary (citable) accession number: C8NRH0
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: February 4, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

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.