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Protein

Pyridoxamine--pyruvate transaminase

Gene

ppaT

more
Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a reversible transamination reaction between pyridoxamine and pyruvate to form pyridoxal and L-alanine.2 Publications

Catalytic activityi

Pyridoxamine + pyruvate = pyridoxal + L-alanine.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Kineticsi

kcat is 28 sec(-1) for pyridoxamine. kcat is 41 sec(-1) for pyridoxal. kcat is 29 sec(-1) for pyruvate. kcat is 24 sec(-1) for 2-oxobutyrate. kcat is 41 sec(-1) for L-alanine. kcat is 9 sec(-1) for (S)-2-aminobutyrate.

  1. KM=0.044 mM for pyridoxamine1 Publication
  2. KM=0.059 mM for pyridoxal1 Publication
  3. KM=0.34 mM for pyruvate1 Publication
  4. KM=7.1 mM for 2-oxobutyrate1 Publication
  5. KM=11 mM for L-alanine1 Publication
  6. KM=20 mM for (S)-2-aminobutyrate1 Publication

    pH dependencei

    Optimum pH is 9.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei68 – 681Pyridoxal phosphate1 Publication
    Binding sitei95 – 951Pyridoxal phosphate1 Publication
    Binding sitei146 – 1461Pyridoxal phosphate1 Publication
    Binding sitei345 – 3451Pyridoxal phosphate1 Publication

    GO - Molecular functioni

    • pyridoxal phosphate binding Source: UniProtKB
    • pyridoxamine-pyruvate transaminase activity Source: UniProtKB-EC
    • transaminase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Chloride, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13150.
    MLOT266835:GJ9L-5397-MONOMER.
    BRENDAi2.6.1.30. 3243.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyridoxamine--pyruvate transaminase (EC:2.6.1.30)
    Alternative name(s):
    Pyridoxamine-pyruvate aminotransferase
    Gene namesi
    Name:ppaT
    AND
    Ordered Locus Names:mlr6806
    OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
    Taxonomic identifieri266835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
    Proteomesi
    • UP000000552 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681E → A or G: Low but detectable pyridoxamine--pyruvate transaminase activity. 1 Publication
    Mutagenesisi197 – 1971K → L: Loss of function. 1 Publication
    Mutagenesisi198 – 1981C → A: No effect on enzyme activity. 1 Publication
    Mutagenesisi336 – 3361R → A: Strongly deacreased affinity for pyruvate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 393392Pyridoxamine--pyruvate transaminasePRO_0000430257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei197 – 1971N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi266835.mlr6806.

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 133Combined sources
    Beta strandi15 – 173Combined sources
    Helixi23 – 286Combined sources
    Helixi39 – 5517Combined sources
    Beta strandi63 – 675Combined sources
    Helixi70 – 8011Combined sources
    Beta strandi87 – 937Combined sources
    Helixi94 – 10613Combined sources
    Beta strandi110 – 1145Combined sources
    Helixi123 – 13210Combined sources
    Beta strandi138 – 1447Combined sources
    Helixi146 – 1483Combined sources
    Helixi154 – 16310Combined sources
    Beta strandi167 – 1715Combined sources
    Turni173 – 1753Combined sources
    Helixi183 – 1864Combined sources
    Beta strandi189 – 1935Combined sources
    Beta strandi195 – 1973Combined sources
    Beta strandi206 – 2105Combined sources
    Helixi212 – 2198Combined sources
    Helixi233 – 2353Combined sources
    Turni236 – 2394Combined sources
    Helixi251 – 26717Combined sources
    Helixi269 – 28921Combined sources
    Beta strandi294 – 2985Combined sources
    Helixi299 – 3013Combined sources
    Beta strandi306 – 3105Combined sources
    Helixi317 – 32812Combined sources
    Helixi337 – 3393Combined sources
    Turni340 – 3423Combined sources
    Beta strandi343 – 3475Combined sources
    Helixi350 – 3523Combined sources
    Helixi355 – 37117Combined sources
    Helixi378 – 39215Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z9UX-ray2.00A/B2-393[»]
    2Z9VX-ray1.70A/B2-393[»]
    2Z9WX-ray1.70A/B2-393[»]
    2Z9XX-ray1.94A/B2-393[»]
    ProteinModelPortaliQ988B8.
    SMRiQ988B8. Positions 2-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ988B8.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C5R. Bacteria.
    COG0075. LUCA.
    HOGENOMiHOG000171814.
    KOiK18608.
    OMAiQKAMGGP.
    OrthoDBiPOG091H03C8.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000192. Aminotrans_V_dom.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q988B8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMRYPEHADP VITLTAGPVN AYPEVLRGLG RTVLYDYDPA FQLLYEKVVD
    60 70 80 90 100
    KAQKAMRLSN KPVILHGEPV LGLEAAAASL ISPDDVVLNL ASGVYGKGFG
    110 120 130 140 150
    YWAKRYSPHL LEIEVPYNEA IDPQAVADML KAHPEITVVS VCHHDTPSGT
    160 170 180 190 200
    INPIDAIGAL VSAHGAYLIV DAVSSFGGMK THPEDCKADI YVTGPNKCLG
    210 220 230 240 250
    APPGLTMMGV SERAWAKMKA NPLAPRASML SIVDWENAWS RDKPFPFTPS
    260 270 280 290 300
    VSEINGLDVA LDLYLNEGPE AVWARHALTA KAMRAGVTAM GLSVWAASDS
    310 320 330 340 350
    IASPTTTAVR TPDGVDEKAL RQAARARYGV VFSSGRGETL GKLTRIGHMG
    360 370 380 390
    PTAQPIYAIA ALTALGGAMN AAGRKLAIGK GIEAALAVID ADA
    Length:393
    Mass (Da):41,590
    Last modified:October 1, 2001 - v1
    Checksum:iEB25E53E28C0AB61
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB195265 Genomic DNA. Translation: BAE48518.1.
    BA000012 Genomic DNA. Translation: BAB53032.1.

    Genome annotation databases

    EnsemblBacteriaiBAB53032; BAB53032; BAB53032.
    KEGGimlo:mlr6806.
    PATRICi22485073. VBIMesLot2464_5416.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB195265 Genomic DNA. Translation: BAE48518.1.
    BA000012 Genomic DNA. Translation: BAB53032.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z9UX-ray2.00A/B2-393[»]
    2Z9VX-ray1.70A/B2-393[»]
    2Z9WX-ray1.70A/B2-393[»]
    2Z9XX-ray1.94A/B2-393[»]
    ProteinModelPortaliQ988B8.
    SMRiQ988B8. Positions 2-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi266835.mlr6806.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB53032; BAB53032; BAB53032.
    KEGGimlo:mlr6806.
    PATRICi22485073. VBIMesLot2464_5416.

    Phylogenomic databases

    eggNOGiENOG4105C5R. Bacteria.
    COG0075. LUCA.
    HOGENOMiHOG000171814.
    KOiK18608.
    OMAiQKAMGGP.
    OrthoDBiPOG091H03C8.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13150.
    MLOT266835:GJ9L-5397-MONOMER.
    BRENDAi2.6.1.30. 3243.

    Miscellaneous databases

    EvolutionaryTraceiQ988B8.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000192. Aminotrans_V_dom.
    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.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPPAT_RHILO
    AccessioniPrimary (citable) accession number: Q988B8
    Secondary accession number(s): Q2Z2G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: October 1, 2001
    Last modified: September 7, 2016
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.