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P0A790

- PAND_ECOLI

UniProt

P0A790 - PAND_ECOLI

Protein

Aspartate 1-decarboxylase

Gene

panD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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-SubCell

    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.
    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

    MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT    50
    NGKRFSTYAI AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART 100
    WRPNVAYFEG DNEMKRTAKA IPVQVA 126
    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.
    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

    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 1, 2014
    This is version 90 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