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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)DescriptionActionsGraphical viewLength
    Binding sitei92Pyridoxal phosphate1
    Binding sitei143Pyridoxal phosphate1
    Binding sitei168Pyridoxal phosphate1
    Binding sitei243Pyridoxal phosphate1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate, Pyruvate

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi168D → A: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi194K → L or R: Loss of enzymatic activity. 1 Publication1
    Mutagenesisi340R → A or K: Decreased affinity for all of the substrates. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002867872 – 3672-aminoethylphosphonate--pyruvate transaminaseAdd BLAST366

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei194N6-(pyridoxal phosphate)lysineSequence analysis1

    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

    1367
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 13Combined sources4
    Helixi18 – 22Combined sources5
    Helixi33 – 36Combined sources4
    Turni37 – 39Combined sources3
    Helixi40 – 51Combined sources12
    Beta strandi53 – 64Combined sources12
    Helixi66 – 76Combined sources11
    Beta strandi84 – 90Combined sources7
    Helixi91 – 103Combined sources13
    Beta strandi107 – 111Combined sources5
    Helixi120 – 129Combined sources10
    Beta strandi135 – 141Combined sources7
    Turni143 – 145Combined sources3
    Helixi151 – 161Combined sources11
    Beta strandi164 – 168Combined sources5
    Turni170 – 175Combined sources6
    Turni180 – 184Combined sources5
    Beta strandi186 – 194Combined sources9
    Beta strandi200 – 208Combined sources9
    Helixi209 – 212Combined sources4
    Helixi226 – 235Combined sources10
    Turni236 – 238Combined sources3
    Helixi246 – 262Combined sources17
    Helixi264 – 285Combined sources22
    Beta strandi290 – 292Combined sources3
    Helixi294 – 296Combined sources3
    Beta strandi299 – 305Combined sources7
    Helixi314 – 323Combined sources10
    Beta strandi334 – 336Combined sources3
    Beta strandi338 – 342Combined sources5
    Helixi349 – 362Combined sources14

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP96060.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni65 – 67Pyridoxal phosphate binding3

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1M32X-ray2.20A/B/C/D/E/F2-367[»]
    ProteinModelPortaliP96060.
    SMRiP96060.
    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.

    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: November 2, 2016
    This is version 104 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.