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P0A790

- PAND_ECOLI

UniProt

P0A790 - PAND_ECOLI

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Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.1 Publication

Catalytic activityi

L-aspartate = beta-alanine + CO2.1 Publication

Cofactori

Pyruvoyl group.

Enzyme regulationi

Inhibited by hydroxylamine, phenylhydrazine, sodium borohydride, D-cycloserine, hydrazine, semicarbazine and succinic dehydrazine. L-glutamate, succinate, oxaloacetate, L-serine, L-cysteic acid, beta-hydroxy-DL-asparate, and D-serine are competitive inhibitors (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251Schiff-base intermediate with substrate; via pyruvic acid
Binding sitei57 – 571SubstrateBy similarity
Active sitei58 – 581Proton donor

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
  3. protein autoprocessing Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciEcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.
BRENDAi4.1.1.11. 2026.
UniPathwayiUPA00028; UER00002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate 1-decarboxylase (EC:4.1.1.11)
Alternative name(s):
Aspartate alpha-decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Name:panD
Ordered Locus Names:b0131, JW0127
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11747. panD.

Subcellular locationi

Cytoplasm 1 Publication

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 chainPRO_0000023073Add
BLAST
Chaini25 – 126102Aspartate 1-decarboxylase alpha chainPRO_0000023074Add
BLAST

Amino acid modifications

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

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.

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

PRIDEiP0A790.

Expressioni

Gene expression databases

GenevestigatoriP0A790.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta subunits.1 Publication

Protein-protein interaction databases

IntActiP0A790. 2 interactions.
STRINGi511145.b0131.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1413
Beta strandi17 – 193
Beta strandi20 – 223
Beta strandi26 – 294
Helixi30 – 367
Beta strandi43 – 486
Turni49 – 513
Beta strandi54 – 629
Beta strandi69 – 724
Helixi73 – 775
Beta strandi84 – 9411
Helixi95 – 984
Beta strandi104 – 1096
Turni110 – 1123
Beta strandi113 – 1175
Helixi118 – 1203

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW8X-ray2.20A/D1-24[»]
B/E25-115[»]
1PPYX-ray1.95A/B1-126[»]
1PQEX-ray1.95A1-126[»]
1PQFX-ray2.00A/B1-126[»]
1PQHX-ray1.29A/B1-126[»]
1PT0X-ray2.00A/B1-126[»]
1PT1X-ray1.90A/B1-126[»]
1PYQX-ray1.90A/B1-126[»]
1PYUX-ray1.90A/C1-24[»]
B/D25-126[»]
3TM7X-ray1.70A/C1-24[»]
B/D25-126[»]
4AOKX-ray1.50A/D1-24[»]
B/E26-126[»]
4AONX-ray1.50A/D1-24[»]
B/E25-126[»]
4AZDX-ray1.62A/B1-126[»]
ProteinModelPortaliP0A790.
SMRiP0A790. Positions 25-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A790.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the PanD family.Curated

Phylogenomic databases

HOGENOMiHOG000221007.
InParanoidiP0A790.
KOiK01579.
OMAiWYDGSCA.
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.

P0A790-1 [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071Y → N(PubMed:8202364)Curated
Sequence conflicti120 – 1212AI → TV(PubMed:8202364)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17086 Genomic DNA. Translation: AAA24274.1.
U00096 Genomic DNA. Translation: AAC73242.1.
AP009048 Genomic DNA. Translation: BAB96708.2.
PIRiC64736.
RefSeqiNP_414673.1. NC_000913.3.
YP_488434.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73242; AAC73242; b0131.
BAB96708; BAB96708; BAB96708.
GeneIDi12930736.
945686.
KEGGiecj:Y75_p0128.
eco:b0131.
PATRICi32115365. VBIEscCol129921_0134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17086 Genomic DNA. Translation: AAA24274.1 .
U00096 Genomic DNA. Translation: AAC73242.1 .
AP009048 Genomic DNA. Translation: BAB96708.2 .
PIRi C64736.
RefSeqi NP_414673.1. NC_000913.3.
YP_488434.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AW8 X-ray 2.20 A/D 1-24 [» ]
B/E 25-115 [» ]
1PPY X-ray 1.95 A/B 1-126 [» ]
1PQE X-ray 1.95 A 1-126 [» ]
1PQF X-ray 2.00 A/B 1-126 [» ]
1PQH X-ray 1.29 A/B 1-126 [» ]
1PT0 X-ray 2.00 A/B 1-126 [» ]
1PT1 X-ray 1.90 A/B 1-126 [» ]
1PYQ X-ray 1.90 A/B 1-126 [» ]
1PYU X-ray 1.90 A/C 1-24 [» ]
B/D 25-126 [» ]
3TM7 X-ray 1.70 A/C 1-24 [» ]
B/D 25-126 [» ]
4AOK X-ray 1.50 A/D 1-24 [» ]
B/E 26-126 [» ]
4AON X-ray 1.50 A/D 1-24 [» ]
B/E 25-126 [» ]
4AZD X-ray 1.62 A/B 1-126 [» ]
ProteinModelPortali P0A790.
SMRi P0A790. Positions 25-122.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A790. 2 interactions.
STRINGi 511145.b0131.

Proteomic databases

PRIDEi P0A790.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73242 ; AAC73242 ; b0131 .
BAB96708 ; BAB96708 ; BAB96708 .
GeneIDi 12930736.
945686.
KEGGi ecj:Y75_p0128.
eco:b0131.
PATRICi 32115365. VBIEscCol129921_0134.

Organism-specific databases

EchoBASEi EB1697.
EcoGenei EG11747. panD.

Phylogenomic databases

HOGENOMi HOG000221007.
InParanoidi P0A790.
KOi K01579.
OMAi WYDGSCA.
OrthoDBi EOG6P5ZMC.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00002 .
BioCyci EcoCyc:ASPDECARBOX-MONOMER.
ECOL316407:JW0127-MONOMER.
MetaCyc:ASPDECARBOX-MONOMER.
BRENDAi 4.1.1.11. 2026.

Miscellaneous databases

EvolutionaryTracei P0A790.
PROi P0A790.

Gene expression databases

Genevestigatori P0A790.

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

« Hide 'large scale' publications
  1. "Characterization and sequence of the Escherichia coli panBCD gene cluster."
    Merkel W.K., Nichols B.P.
    FEMS Microbiol. Lett. 143:247-252(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 107 AND 120-121.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry."
    Ramjee M.K., Genschel U., Abell C., Smith A.G.
    Biochem. J. 323:661-669(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-5 AND 25-29, CHARACTERIZATION.
  6. "Beta-alanine synthesis in Escherichia coli."
    Cronan J.E. Jr.
    J. Bacteriol. 141:1291-1297(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  7. "Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction."
    Saldanha S.A., Birch L.M., Webb M.E., Nabbs B.K., von Delft F., Smith A.G., Abell C.
    Chem. Commun. (Camb.) 18:1760-1761(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME MECHANISM.
  8. "Crystal structure of aspartate decarboxylase at 2.2-A resolution provides evidence for an ester in protein self-processing."
    Albert A., Dhanaraj V., Genschel U., Khan G., Ramjee M.K., Pulido R., Sibanda B.L., von Delft F., Witty M., Blundell T.L., Smith A.G., Abell C.
    Nat. Struct. Biol. 5:289-293(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-115, PROTEOLYTIC PROCESSING BY SELF, SUBUNIT.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS), PROTEOLYTIC PROCESSING BY SELF.

Entry informationi

Entry nameiPAND_ECOLI
AccessioniPrimary (citable) accession number: P0A790
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 91 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3