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P0A793

- PAND_SHIFL

UniProt

P0A793 - PAND_SHIFL

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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Shigella flexneri
Status
Reviewed - 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

Pyruvoyl group.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

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:SF0128, S0130
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2424Aspartate 1-decarboxylase beta chainUniRule annotationPRO_0000023155Add
BLAST
Chaini25 – 126102Aspartate 1-decarboxylase alpha chainUniRule annotationPRO_0000023156Add
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

Proteomic databases

PaxDbiP0A793.
PRIDEiP0A793.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF0128.

Structurei

3D structure databases

ProteinModelPortaliP0A793.
SMRiP0A793. Positions 25-122.
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.
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.

P0A793-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT
60 70 80 90 100
NGKRFSTYAI AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART
110 120
WRPNVAYFEG DNEMKRTAKA IPVQVA
Length:126
Mass (Da):13,834
Last modified:June 7, 2005 - v1
Checksum:iE3169F5C2BDD5D25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41791.2.
AE014073 Genomic DNA. Translation: AAP15672.1.
RefSeqiNP_706084.2. NC_004337.2.
NP_835867.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN41791; AAN41791; SF0128.
AAP15672; AAP15672; S0130.
GeneIDi1024489.
1076562.
KEGGisfl:SF0128.
sfx:S0130.
PATRICi18701202. VBIShiFle31049_0143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN41791.2 .
AE014073 Genomic DNA. Translation: AAP15672.1 .
RefSeqi NP_706084.2. NC_004337.2.
NP_835867.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0A793.
SMRi P0A793. Positions 25-122.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF0128.

Proteomic databases

PaxDbi P0A793.
PRIDEi P0A793.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN41791 ; AAN41791 ; SF0128 .
AAP15672 ; AAP15672 ; S0130 .
GeneIDi 1024489.
1076562.
KEGGi sfl:SF0128.
sfx:S0130.
PATRICi 18701202. VBIShiFle31049_0143.

Phylogenomic databases

eggNOGi COG0853.
HOGENOMi HOG000221007.
KOi K01579.
OrthoDBi EOG6P5ZMC.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00002 .

Family and domain databases

HAMAPi MF_00446. PanD.
InterProi IPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view ]
PANTHERi PTHR21012. PTHR21012. 1 hit.
Pfami PF02261. Asp_decarbox. 1 hit.
[Graphical view ]
PIRSFi PIRSF006246. Asp_decarbox. 1 hit.
ProDomi PD009294. Asp_decarbox. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR00223. panD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiPAND_SHIFL
AccessioniPrimary (citable) accession number: P0A793
Secondary accession number(s): P31664, Q8KMY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 69 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

Documents

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

External Data

Dasty 3