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Protein

Phosphonoacetaldehyde hydrolase

Gene

phnX

Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in phosphonate degradation.

Catalytic activityi

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Kineticsi

  1. KM=33 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei9Nucleophile1
    Metal bindingi9Magnesium1
    Metal bindingi11Magnesium; via carbonyl oxygen1
    Active sitei50Schiff-base intermediate with substrate1
    Metal bindingi183Magnesium1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Schiff base

    Enzyme and pathway databases

    BRENDAi3.11.1.1. 648.
    SABIO-RKO31156.

    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
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi9D → A: Loss of enzymatic activity. 2 Publications1
    Mutagenesisi9D → E: Kcat/KM decreases 30000-fold. 2 Publications1
    Mutagenesisi19C → A or S: Kcat/KM decreases 10-100-fold. 1 Publication1
    Mutagenesisi46M → L: Kcat/KM decreases 17000-fold. 1 Publication1
    Mutagenesisi47G → A: Kcat/KM decreases 10000-fold. 1 Publication1
    Mutagenesisi47G → P or V: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi50K → R: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi53H → A: Kcat/KM decreases 1000-fold. 2 Publications1
    Mutagenesisi53H → Q: Kcat/KM decreases 250-fold. 2 Publications1
    Mutagenesisi125Y → A: Kcat/KM decreases 230-fold. 1 Publication1
    Mutagenesisi125Y → F: Kcat/KM decreases 10-fold. 1 Publication1
    Mutagenesisi183D → A: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi187D → A: Kcat/KM decreases 10000-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002845751 – 264Phosphonoacetaldehyde hydrolaseAdd BLAST264

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Structurei

    Secondary structure

    1264
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 8Combined sources4
    Turni11 – 13Combined sources3
    Beta strandi14 – 16Combined sources3
    Helixi23 – 31Combined sources9
    Turni32 – 34Combined sources3
    Helixi39 – 43Combined sources5
    Turni44 – 47Combined sources4
    Helixi50 – 59Combined sources10
    Helixi61 – 71Combined sources11
    Helixi77 – 94Combined sources18
    Helixi95 – 98Combined sources4
    Helixi105 – 114Combined sources10
    Beta strandi118 – 122Combined sources5
    Helixi127 – 139Combined sources13
    Beta strandi145 – 147Combined sources3
    Helixi150 – 152Combined sources3
    Beta strandi153 – 155Combined sources3
    Beta strandi157 – 160Combined sources4
    Helixi161 – 170Combined sources10
    Helixi175 – 177Combined sources3
    Beta strandi178 – 184Combined sources7
    Helixi185 – 193Combined sources9
    Beta strandi196 – 201Combined sources6
    Turni206 – 208Combined sources3
    Helixi212 – 217Combined sources6
    Helixi220 – 236Combined sources17
    Beta strandi240 – 245Combined sources6
    Helixi246 – 248Combined sources3
    Helixi249 – 256Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FEZX-ray3.00A/B/C/D2-257[»]
    1RDFX-ray2.80A/B/C/D/E/F1-264[»]
    1RQLX-ray2.40A/B1-264[»]
    1RQNX-ray2.80A/B1-264[»]
    1SWVX-ray2.30A/B1-264[»]
    1SWWX-ray2.30A/B1-264[»]
    2IOFX-ray2.50A/K1-264[»]
    2IOHX-ray2.90A/B/C/D1-264[»]
    ProteinModelPortaliO31156.
    SMRiO31156.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO31156.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    HAMAPiMF_01375. PhnX. 1 hit.
    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.
    TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR01422. phosphonatase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O31156-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIEAVIFDW AGTTVDYGCF APLEVFMEIF HKRGVAITAE EARKPMGLLK
    60 70 80 90 100
    IDHVRALTEM PRIASEWNRV FRQLPTEADI QEMYEEFEEI LFAILPRYAS
    110 120 130 140 150
    PINGVKEVIA SLRERGIKIG STTGYTREMM DIVAKEAALQ GYKPDFLVTP
    160 170 180 190 200
    DDVPAGRPYP WMCYKNAMEL GVYPMNHMIK VGDTVSDMKE GRNAGMWTVG
    210 220 230 240 250
    VILGSSELGL TEEEVENMDS VELREKIEVV RNRFVENGAH FTIETMQELE
    260
    SVMEHIEKQE LIIS
    Length:264
    Mass (Da):30,060
    Last modified:April 17, 2007 - v3
    Checksum:i59A99D2BBED760AD
    GO

    Sequence cautioni

    The sequence AAB86434 differs from that shown. Reason: Erroneous initiation.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030979 Genomic DNA. Translation: AAB86434.2. Different initiation.
    RefSeqiWP_000687366.1. NZ_LJKC01000028.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF030979 Genomic DNA. Translation: AAB86434.2. Different initiation.
    RefSeqiWP_000687366.1. NZ_LJKC01000028.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FEZX-ray3.00A/B/C/D2-257[»]
    1RDFX-ray2.80A/B/C/D/E/F1-264[»]
    1RQLX-ray2.40A/B1-264[»]
    1RQNX-ray2.80A/B1-264[»]
    1SWVX-ray2.30A/B1-264[»]
    1SWWX-ray2.30A/B1-264[»]
    2IOFX-ray2.50A/K1-264[»]
    2IOHX-ray2.90A/B/C/D1-264[»]
    ProteinModelPortaliO31156.
    SMRiO31156.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.11.1.1. 648.
    SABIO-RKO31156.

    Miscellaneous databases

    EvolutionaryTraceiO31156.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    HAMAPiMF_01375. PhnX. 1 hit.
    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.
    TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR01422. phosphonatase. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPHNX_BACCE
    AccessioniPrimary (citable) accession number: O31156
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: November 2, 2016
    This is version 79 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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

    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 one 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.