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Protein

2-aminoethylphosphonate--pyruvate transaminase

Gene

phnW

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

Functioni

Involved in phosphonate degradation.

Catalytic activityi

(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine.

Cofactori

pyridoxal 5'-phosphate1 PublicationNote: Thr-243 of one partner binds the pyridoxal phosphate moiety of the other.1 Publication

Kineticsi

  1. KM=1.11 mM for (2-aminoethyl)phosphonate (at 25 degrees Celsius, pH 8.5)
  2. KM=0.15 mM for pyruvate (at 25 degrees Celsius, pH 8.5)
  3. KM=0.09 mM for 2-phosphonoacetaldehyde (at 25 degrees Celsius, pH 8.5)
  4. KM=1.4 mM for L-alanine (at 25 degrees Celsius, pH 8.5)

    pH dependencei

    Optimum pH is 6.5-9.5 for phosphonoacetaldehyde formation, and 7.5-8.5 for 2-aminoethyl phosphonate formation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Pyridoxal phosphate
    Binding sitei143 – 1431Pyridoxal phosphate
    Binding sitei168 – 1681Pyridoxal phosphate
    Binding sitei243 – 2431Pyridoxal phosphate

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate, Pyruvate

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-432-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-aminoethylphosphonate--pyruvate transaminase (EC:2.6.1.37)
    Alternative name(s):
    2-aminoethylphosphonate aminotransferase
    AEP transaminase
    Short name:
    AEPT
    Gene namesi
    Name:phnW
    Ordered Locus Names:STM0431
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681D → A: Loss of enzymatic activity. 1 Publication
    Mutagenesisi194 – 1941K → L or R: Loss of enzymatic activity. 1 Publication
    Mutagenesisi340 – 3401R → A or K: Decreased affinity for all of the substrates. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 3673662-aminoethylphosphonate--pyruvate transaminasePRO_0000286787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-(pyridoxal phosphate)lysineSequence analysis

    Proteomic databases

    PaxDbiP96060.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi99287.STM0431.

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 134Combined sources
    Helixi18 – 225Combined sources
    Helixi33 – 364Combined sources
    Turni37 – 393Combined sources
    Helixi40 – 5112Combined sources
    Beta strandi53 – 6412Combined sources
    Helixi66 – 7611Combined sources
    Beta strandi84 – 907Combined sources
    Helixi91 – 10313Combined sources
    Beta strandi107 – 1115Combined sources
    Helixi120 – 12910Combined sources
    Beta strandi135 – 1417Combined sources
    Turni143 – 1453Combined sources
    Helixi151 – 16111Combined sources
    Beta strandi164 – 1685Combined sources
    Turni170 – 1756Combined sources
    Turni180 – 1845Combined sources
    Beta strandi186 – 1949Combined sources
    Beta strandi200 – 2089Combined sources
    Helixi209 – 2124Combined sources
    Helixi226 – 23510Combined sources
    Turni236 – 2383Combined sources
    Helixi246 – 26217Combined sources
    Helixi264 – 28522Combined sources
    Beta strandi290 – 2923Combined sources
    Helixi294 – 2963Combined sources
    Beta strandi299 – 3057Combined sources
    Helixi314 – 32310Combined sources
    Beta strandi334 – 3363Combined sources
    Beta strandi338 – 3425Combined sources
    Helixi349 – 36214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M32X-ray2.20A/B/C/D/E/F2-367[»]
    ProteinModelPortaliP96060.
    SMRiP96060. Positions 5-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96060.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 673Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107STF. Bacteria.
    COG0075. LUCA.
    HOGENOMiHOG000171816.
    KOiK03430.
    OMAiKFGQRWV.
    PhylomeDBiP96060.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01376. PhnW_aminotrans_5. 1 hit.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR012703. NH2EtPonate_pyrv_transaminase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR024169. SP_NH2Trfase/AEP_transaminase.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000524. SPT. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03301. PhnW-AepZ. 1 hit.
    TIGR02326. transamin_PhnW. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P96060-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSRNYLLLT PGPLTTSRTV KEAMLFDSCT WDDDYNIGVV EQIRQQLTAL
    60 70 80 90 100
    ATASEGYTSV LLQGSGSYAV EAVLGSALGP QDKVLIVSNG AYGARMVEMA
    110 120 130 140 150
    GLMGIAHHAY DCGEVARPDV QAIDAILNAD PTISHIAMVH SETTTGMLNP
    160 170 180 190 200
    IDEVGALAHR YGKTYIVDAM SSFGGIPMDI AALHIDYLIS SANKCIQGVP
    210 220 230 240 250
    GFAFVIAREQ KLAACKGHSR SLSLDLYAQW RCMEDNHGKW RFTSPTHTVL
    260 270 280 290 300
    AFAQALKELA KEGGVAARHQ RYQQNQRSLV AGMRALGFNT LLDDELHSPI
    310 320 330 340 350
    ITAFYSPEDP QYRFSEFYRR LKEQGFVIYP GKVSQSDCFR IGNIGEVYAA
    360
    DITALLTAIR TAMYWTK
    Length:367
    Mass (Da):40,249
    Last modified:May 1, 1997 - v1
    Checksum:iF7D00905816480BE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U69493 Genomic DNA. Translation: AAB39642.1.
    AE006468 Genomic DNA. Translation: AAL19385.1.
    PIRiT46947.
    RefSeqiNP_459426.1. NC_003197.1.
    WP_000203955.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL19385; AAL19385; STM0431.
    GeneIDi1251950.
    KEGGistm:STM0431.
    PATRICi32379197. VBISalEnt20916_0460.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U69493 Genomic DNA. Translation: AAB39642.1.
    AE006468 Genomic DNA. Translation: AAL19385.1.
    PIRiT46947.
    RefSeqiNP_459426.1. NC_003197.1.
    WP_000203955.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M32X-ray2.20A/B/C/D/E/F2-367[»]
    ProteinModelPortaliP96060.
    SMRiP96060. Positions 5-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM0431.

    Proteomic databases

    PaxDbiP96060.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL19385; AAL19385; STM0431.
    GeneIDi1251950.
    KEGGistm:STM0431.
    PATRICi32379197. VBISalEnt20916_0460.

    Phylogenomic databases

    eggNOGiENOG4107STF. Bacteria.
    COG0075. LUCA.
    HOGENOMiHOG000171816.
    KOiK03430.
    OMAiKFGQRWV.
    PhylomeDBiP96060.

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-432-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP96060.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01376. PhnW_aminotrans_5. 1 hit.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR012703. NH2EtPonate_pyrv_transaminase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR024169. SP_NH2Trfase/AEP_transaminase.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000524. SPT. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03301. PhnW-AepZ. 1 hit.
    TIGR02326. transamin_PhnW. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPHNW_SALTY
    AccessioniPrimary (citable) accession number: P96060
    Secondary accession number(s): Q7CR29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 1, 1997
    Last modified: September 7, 2016
    This is version 102 of the entry and version 1 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.

    Caution

    The crystal structure does not show the Schiff base that is expected to form between Lys-194 and the pyridoxal phosphate cofactor.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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.