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P51016

- HOA_PSEUF

UniProt

P51016 - HOA_PSEUF

Protein

4-hydroxy-2-oxovalerate aldolase

Gene

dmpG

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols.1 PublicationUniRule annotation

    Catalytic activityi

    (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate.1 PublicationUniRule annotation

    Enzyme regulationi

    Six- to eight-fold activated by Mn2+. Retains residual activity after EDTA treatment in vitro. Also activated by NADH and, to a lesser extent, by NAD+. Strongly inhibited by Zn2+. Mg2+ and Ca2+ have no effect on enzymatic activity.1 Publication

    pH dependencei

    Optimum pH is 8.5-9.0.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei17 – 171Transition state stabilizerUniRule annotation
    Metal bindingi18 – 181Manganese1 PublicationUniRule annotation
    Active sitei21 – 211Proton acceptorUniRule annotation
    Binding sitei171 – 1711Substrate
    Metal bindingi200 – 2001Manganese; via tele nitrogen1 PublicationUniRule annotation
    Binding sitei200 – 2001Substrate
    Metal bindingi202 – 2021Manganese; via tele nitrogen1 PublicationUniRule annotation
    Binding sitei291 – 2911Substrate

    GO - Molecular functioni

    1. 4-hydroxy-2-oxovalerate aldolase activity Source: UniProtKB
    2. manganese ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB
    2. benzoate catabolic process via hydroxylation Source: UniProtKB-UniPathway
    3. phenol-containing compound catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12778.
    UniPathwayiUPA00156.
    UPA00728.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxy-2-oxovalerate aldolaseUniRule annotation (EC:4.1.3.39UniRule annotation)
    Short name:
    HOAUniRule annotation
    Alternative name(s):
    4-hydroxy-2-keto-pentanoic acid aldolaseUniRule annotation
    4-hydroxy-2-oxopentanoate aldolaseUniRule annotation
    Gene namesi
    Name:dmpG
    Encoded oniPlasmid pVI1500 Publication
    OrganismiPseudomonas sp. (strain CF600)
    Taxonomic identifieri79676 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 3453444-hydroxy-2-oxovalerate aldolasePRO_0000079938Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites.2 Publications

    Protein-protein interaction databases

    IntActiP51016. 1 interaction.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 134
    Turni15 – 173
    Helixi18 – 225
    Turni23 – 253
    Helixi29 – 4214
    Beta strandi45 – 484
    Turni60 – 623
    Helixi69 – 779
    Beta strandi81 – 899
    Helixi96 – 10510
    Beta strandi109 – 1157
    Helixi119 – 1224
    Helixi123 – 13210
    Beta strandi135 – 1428
    Helixi148 – 16114
    Beta strandi164 – 1696
    Helixi177 – 19014
    Beta strandi195 – 2006
    Helixi208 – 21710
    Beta strandi222 – 2265
    Helixi227 – 2293
    Helixi239 – 24911
    Helixi257 – 26610
    Helixi269 – 2713
    Helixi280 – 2889
    Helixi294 – 30512
    Helixi309 – 31911
    Helixi327 – 34014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NVMX-ray1.70A/C/E/G1-345[»]
    ProteinModelPortaliP51016.
    SMRiP51016. Positions 2-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51016.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 182Substrate binding

    Sequence similaritiesi

    Belongs to the 4-hydroxy-2-oxovalerate aldolase family.UniRule annotation

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01656. HOA.
    InterProiIPR017629. 4OH_2_O-val_aldolase.
    IPR013785. Aldolase_TIM.
    IPR012425. DmpG_comm.
    IPR000891. PYR_CT.
    [Graphical view]
    PANTHERiPTHR10277:SF3. PTHR10277:SF3. 1 hit.
    PfamiPF07836. DmpG_comm. 1 hit.
    PF00682. HMGL-like. 1 hit.
    [Graphical view]
    ProDomiPD005364. DmpG_comm. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    TIGRFAMsiTIGR03217. 4OH_2_O_val_ald. 1 hit.
    PROSITEiPS50991. PYR_CT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P51016-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTFNPSKKLY ISDVTLRDGS HAIRHQYTLD DVRAIARALD KAKVDSIEVA    50
    HGDGLQGSSF NYGFGRHTDL EYIEAVAGEI SHAQIATLLL PGIGSVHDLK 100
    NAYQAGARVV RVATHCTEAD VSKQHIEYAR NLGMDTVGFL MMSHMIPAEK 150
    LAEQGKLMES YGATCIYMAD SGGAMSMNDI RDRMRAFKAV LKPETQVGMH 200
    AHHNLSLGVA NSIVAVEEGC DRVDASLAGM GAGAGNAPLE VFIAVAERLG 250
    WNHGTDLYTL MDAADDIVRP LQDRPVRVDR ETLGLGYAGV YSSFLRHAEI 300
    AAAKYNLKTL DILVELGHRR MVGGQEDMIV DVALDLLAAH KENRA 345
    Length:345
    Mass (Da):37,471
    Last modified:October 1, 1996 - v1
    Checksum:i8B38B37A8A0EFEE0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60835 Genomic DNA. Translation: CAA43227.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60835 Genomic DNA. Translation: CAA43227.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NVM X-ray 1.70 A/C/E/G 1-345 [» ]
    ProteinModelPortali P51016.
    SMRi P51016. Positions 2-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P51016. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00156 .
    UPA00728 .
    BioCyci MetaCyc:MONOMER-12778.

    Miscellaneous databases

    EvolutionaryTracei P51016.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01656. HOA.
    InterProi IPR017629. 4OH_2_O-val_aldolase.
    IPR013785. Aldolase_TIM.
    IPR012425. DmpG_comm.
    IPR000891. PYR_CT.
    [Graphical view ]
    PANTHERi PTHR10277:SF3. PTHR10277:SF3. 1 hit.
    Pfami PF07836. DmpG_comm. 1 hit.
    PF00682. HMGL-like. 1 hit.
    [Graphical view ]
    ProDomi PD005364. DmpG_comm. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    TIGRFAMsi TIGR03217. 4OH_2_O_val_ald. 1 hit.
    PROSITEi PS50991. PYR_CT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600."
      Shingler V., Marklund U., Powlowski J.
      J. Bacteriol. 174:711-724(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: CF600.
    2. "Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600."
      Powlowski J., Sahlman L., Shingler V.
      J. Bacteriol. 175:377-385(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-7, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH DMPF, PH DEPENDENCE.
      Strain: CF600.
    3. "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate."
      Manjasetty B.A., Powlowski J., Vrielink A.
      Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPF; NAD; MANGANESE AND OXALATE, SUBUNIT, REACTION MECHANISM.
      Strain: CF600.

    Entry informationi

    Entry nameiHOA_PSEUF
    AccessioniPrimary (citable) accession number: P51016
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 65 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, Direct protein sequencing, Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3