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P0A6L0

- DEOC_ECOLI

UniProt

P0A6L0 - DEOC_ECOLI

Protein

Deoxyribose-phosphate aldolase

Gene

deoC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.

    Catalytic activityi

    2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei167 – 1671Schiff-base intermediate with acetaldehyde1 Publication
    Active sitei201 – 20111 Publication

    GO - Molecular functioni

    1. deoxyribose-phosphate aldolase activity Source: EcoCyc
    2. lyase activity Source: EcoliWiki

    GO - Biological processi

    1. carbohydrate catabolic process Source: EcoliWiki
    2. cellular response to DNA damage stimulus Source: EcoliWiki
    3. deoxyribonucleotide catabolic process Source: EcoliWiki
    4. deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
    5. nucleobase-containing small molecule interconversion Source: EcoliWiki

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciEcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
    ECOL316407:JW4344-MONOMER.
    MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
    SABIO-RKP0A6L0.
    UniPathwayiUPA00002; UER00468.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyribose-phosphate aldolase (EC:4.1.2.4)
    Short name:
    DERA
    Alternative name(s):
    2-deoxy-D-ribose 5-phosphate aldolase
    Phosphodeoxyriboaldolase
    Short name:
    Deoxyriboaldolase
    Gene namesi
    Name:deoC
    Synonyms:dra, thyR
    Ordered Locus Names:b4381, JW4344
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10221. deoC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 259259Deoxyribose-phosphate aldolasePRO_0000057296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei167 – 1671N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A6L0.
    PRIDEiP0A6L0.

    2D gel databases

    SWISS-2DPAGEP0A6L0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6L0.

    Interactioni

    Subunit structurei

    Monomer and homodimer.

    Protein-protein interaction databases

    IntActiP0A6L0. 8 interactions.
    STRINGi511145.b4381.

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Beta strandi15 – 184
    Helixi26 – 3510
    Beta strandi44 – 474
    Helixi50 – 523
    Helixi53 – 6210
    Beta strandi68 – 758
    Turni76 – 783
    Helixi83 – 9614
    Beta strandi99 – 1046
    Helixi107 – 1115
    Helixi116 – 13116
    Beta strandi135 – 1395
    Helixi142 – 1454
    Helixi148 – 16013
    Beta strandi164 – 1674
    Helixi179 – 19214
    Turni195 – 1973
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Helixi209 – 22315
    Turni230 – 2323
    Beta strandi235 – 2384
    Helixi240 – 2489

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCJX-ray1.10A/B1-259[»]
    1JCLX-ray1.05A/B1-259[»]
    1KTNX-ray1.40A/B1-250[»]
    1P1XX-ray0.99A/B1-259[»]
    ProteinModelPortaliP0A6L0.
    SMRiP0A6L0. Positions 1-250.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6L0.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0274.
    HOGENOMiHOG000241644.
    KOiK01619.
    OMAiCKEACGD.
    OrthoDBiEOG6QZMW5.
    PhylomeDBiP0A6L0.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00592. DeoC_type2.
    InterProiIPR013785. Aldolase_TIM.
    IPR011343. DeoC.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    IPR023649. DeoC_typeII.
    [Graphical view]
    PANTHERiPTHR10889. PTHR10889. 1 hit.
    PfamiPF01791. DeoC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001357. DeoC. 1 hit.
    TIGRFAMsiTIGR00126. deoC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A6L0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP    50
    RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE 100
    VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL 150
    IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF 200
    KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH 250
    GDGKSASSY 259
    Length:259
    Mass (Da):27,734
    Last modified:March 29, 2005 - v1
    Checksum:iABA50C625195D494
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181T → N in CAA26974. (PubMed:6749498)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03224 Genomic DNA. Translation: CAA26974.1.
    U14003 Genomic DNA. Translation: AAA97277.1.
    U00096 Genomic DNA. Translation: AAC77334.1.
    AP009048 Genomic DNA. Translation: BAE78370.1.
    PIRiA01102. ADECD.
    RefSeqiNP_418798.1. NC_000913.3.
    YP_492511.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77334; AAC77334; b4381.
    BAE78370; BAE78370; BAE78370.
    GeneIDi12934356.
    948902.
    KEGGiecj:Y75_p4265.
    eco:b4381.
    PATRICi32124378. VBIEscCol129921_4529.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03224 Genomic DNA. Translation: CAA26974.1 .
    U14003 Genomic DNA. Translation: AAA97277.1 .
    U00096 Genomic DNA. Translation: AAC77334.1 .
    AP009048 Genomic DNA. Translation: BAE78370.1 .
    PIRi A01102. ADECD.
    RefSeqi NP_418798.1. NC_000913.3.
    YP_492511.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JCJ X-ray 1.10 A/B 1-259 [» ]
    1JCL X-ray 1.05 A/B 1-259 [» ]
    1KTN X-ray 1.40 A/B 1-250 [» ]
    1P1X X-ray 0.99 A/B 1-259 [» ]
    ProteinModelPortali P0A6L0.
    SMRi P0A6L0. Positions 1-250.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A6L0. 8 interactions.
    STRINGi 511145.b4381.

    2D gel databases

    SWISS-2DPAGE P0A6L0.

    Proteomic databases

    PaxDbi P0A6L0.
    PRIDEi P0A6L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77334 ; AAC77334 ; b4381 .
    BAE78370 ; BAE78370 ; BAE78370 .
    GeneIDi 12934356.
    948902.
    KEGGi ecj:Y75_p4265.
    eco:b4381.
    PATRICi 32124378. VBIEscCol129921_4529.

    Organism-specific databases

    EchoBASEi EB0217.
    EcoGenei EG10221. deoC.

    Phylogenomic databases

    eggNOGi COG0274.
    HOGENOMi HOG000241644.
    KOi K01619.
    OMAi CKEACGD.
    OrthoDBi EOG6QZMW5.
    PhylomeDBi P0A6L0.

    Enzyme and pathway databases

    UniPathwayi UPA00002 ; UER00468 .
    BioCyci EcoCyc:DEOXYRIBOSE-P-ALD-MONOMER.
    ECOL316407:JW4344-MONOMER.
    MetaCyc:DEOXYRIBOSE-P-ALD-MONOMER.
    SABIO-RK P0A6L0.

    Miscellaneous databases

    EvolutionaryTracei P0A6L0.
    PROi P0A6L0.

    Gene expression databases

    Genevestigatori P0A6L0.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00592. DeoC_type2.
    InterProi IPR013785. Aldolase_TIM.
    IPR011343. DeoC.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    IPR023649. DeoC_typeII.
    [Graphical view ]
    PANTHERi PTHR10889. PTHR10889. 1 hit.
    Pfami PF01791. DeoC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001357. DeoC. 1 hit.
    TIGRFAMsi TIGR00126. deoC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme."
      Valentin-Hansen P., Boetius F., Hammer-Jespersen K., Svendsen I.
      Eur. J. Biochem. 125:561-566(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    6. "Observation of covalent intermediates in an enzyme mechanism at atomic resolution."
      Heine A., DeSantis G., Luz J.G., Mitchell M., Wong C.-H., Wilson I.A.
      Science 294:369-374(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS), ACTIVE SITE, MUTAGENESIS.

    Entry informationi

    Entry nameiDEOC_ECOLI
    AccessioniPrimary (citable) accession number: P0A6L0
    Secondary accession number(s): P00882, Q2M5T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 88 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, 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