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Q7ZAP3

- PHNX_SALTY

UniProt

Q7ZAP3 - PHNX_SALTY

Protein

Phosphonoacetaldehyde hydrolase

Gene

phnX

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Involved in phosphonate degradation.

    Catalytic activityi

    Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate.

    Cofactori

    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

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. phosphonoacetaldehyde hydrolase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. organic phosphonate catabolic process Source: InterPro

    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: 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.
    OMAiGATWEEY.
    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

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    MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL    50
    GKWQHIEALG KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF 100
    SSPIAGVIDT IAALRAEGIK IGSCSGYPRA VMERLVPAAA GHGYRPDHWV 150
    ATDDLAAGGR PGPWMALQNV IALGIDAVAH CVKVDDAAPG ISEGLNAGMW 200
    TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA GAHYVVDSLA 250
    DLPGVIAHIN ARLAQGERP 269
    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.
    The sequence AAL19386.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U69493 Genomic DNA. Translation: AAB39641.1 . Different initiation.
    AE006468 Genomic DNA. Translation: AAL19386.1 . Different initiation.
    PIRi T46946.
    RefSeqi NP_459427.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali Q7ZAP3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM0432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL19386 ; AAL19386 ; STM0432 .
    GeneIDi 1251951.
    KEGGi stm:STM0432.
    PATRICi 32379199. VBISalEnt20916_0461.

    Phylogenomic databases

    eggNOGi COG0637.
    HOGENOMi HOG000217971.
    KOi K05306.
    OMAi GATWEEY.
    OrthoDBi EOG6ZH2FH.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-433-MONOMER.

    Family and domain databases

    Gene3Di 1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    HAMAPi MF_01375. PhnX.
    InterProi IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    IPR006323. Phosphonoacetald_hydro.
    [Graphical view ]
    Pfami PF13419. HAD_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR01422. phosphonatase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 75 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