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Protein

Phosphonoacetaldehyde hydrolase

Gene

phnX

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in phosphonate degradation.

Catalytic activityi

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=40 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei10 – 101NucleophileBy similarity
    Metal bindingi10 – 101MagnesiumBy similarity
    Metal bindingi12 – 121Magnesium; via carbonyl oxygenBy similarity
    Active sitei52 – 521Schiff-base intermediate with substrate
    Metal bindingi186 – 1861MagnesiumBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Schiff base

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-433-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphonoacetaldehyde hydrolase (EC:3.11.1.1)
    Short name:
    Phosphonatase
    Alternative name(s):
    Phosphonoacetaldehyde phosphonohydrolase
    Gene namesi
    Name:phnX
    Ordered Locus Names:STM0432
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521K → R: Complete loss of catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Phosphonoacetaldehyde hydrolasePRO_0000284601Add
    BLAST

    Expressioni

    Inductioni

    Induced when inorganic phosphate is limiting; this is controlled by PhoB.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi99287.STM0432.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7ZAP3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0637.
    HOGENOMiHOG000217971.
    KOiK05306.
    OMAiFDWAGTM.
    OrthoDBiEOG6ZH2FH.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    HAMAPiMF_01375. PhnX.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    IPR006323. Phosphonoacetald_hydro.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR01422. phosphonatase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7ZAP3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL
    60 70 80 90 100
    GKWQHIEALG KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF
    110 120 130 140 150
    SSPIAGVIDT IAALRAEGIK IGSCSGYPRA VMERLVPAAA GHGYRPDHWV
    160 170 180 190 200
    ATDDLAAGGR PGPWMALQNV IALGIDAVAH CVKVDDAAPG ISEGLNAGMW
    210 220 230 240 250
    TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA GAHYVVDSLA
    260
    DLPGVIAHIN ARLAQGERP
    Length:269
    Mass (Da):28,574
    Last modified:April 17, 2007 - v2
    Checksum:i0359B0E1124A3AF3
    GO

    Sequence cautioni

    The sequence AAB39641.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAL19386.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 26524AHYVV…ARLAQ → RITWWIHWRIYL in AAB39641 (PubMed:9649311).CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U69493 Genomic DNA. Translation: AAB39641.1. Different initiation.
    AE006468 Genomic DNA. Translation: AAL19386.1. Different initiation.
    PIRiT46946.
    RefSeqiNP_459427.1. NC_003197.1.
    WP_000981902.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19386; AAL19386; STM0432.
    GeneIDi1251951.
    KEGGistm:STM0432.
    PATRICi32379199. VBISalEnt20916_0461.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U69493 Genomic DNA. Translation: AAB39641.1. Different initiation.
    AE006468 Genomic DNA. Translation: AAL19386.1. Different initiation.
    PIRiT46946.
    RefSeqiNP_459427.1. NC_003197.1.
    WP_000981902.1. NC_003197.1.

    3D structure databases

    ProteinModelPortaliQ7ZAP3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM0432.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL19386; AAL19386; STM0432.
    GeneIDi1251951.
    KEGGistm:STM0432.
    PATRICi32379199. VBISalEnt20916_0461.

    Phylogenomic databases

    eggNOGiCOG0637.
    HOGENOMiHOG000217971.
    KOiK05306.
    OMAiFDWAGTM.
    OrthoDBiEOG6ZH2FH.

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-433-MONOMER.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    HAMAPiMF_01375. PhnX.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    IPR006323. Phosphonoacetald_hydro.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR01422. phosphonatase. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis."
      Baker A.S., Ciocci M.J., Metcalf W.W., Kim J., Babbitt P.C., Wanner B.L., Martin B.M., Dunaway-Mariano D.
      Biochemistry 37:9305-9315(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, BIOPHYSICAL CHARACTERIZATION, REACTION MECHANISM, SCHIFF BASE, MUTAGENESIS OF LYS-52.
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2."
      Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.
      J. Bacteriol. 177:6411-6421(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, CLONING, INDUCTION.
      Strain: LT2.

    Entry informationi

    Entry nameiPHNX_SALTY
    AccessioniPrimary (citable) accession number: Q7ZAP3
    Secondary accession number(s): P96059
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: May 27, 2015
    This is version 78 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Maps to a phosphate-starvation-inducible locus previously known as psiC.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.