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Protein

Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase

Gene

asD

Organism
Pseudomonas sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that has both L-aspartate decarboxylase and transaminase activity. Has high activity with L-aspartate, and much lower activity with D-aspartate, L-lysine and L-glutamine.2 Publications

Catalytic activityi

L-aspartate = L-alanine + CO2.
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Inhibited by 10 mM Co2+, Mn2+ and Ni2+, and by 1 mM Cu2+ and Hg2+.1 Publication

Kineticsi

  1. KM=11 mM for L-aspartate1 Publication

    pH dependencei

    Optimum pH is 5.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei114 – 1141Aspartate; via amide nitrogenBy similarity
    Binding sitei255 – 2551AspartateBy similarity
    Binding sitei496 – 4961AspartateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • alanine biosynthetic process Source: UniProtKB
    • aspartate metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Decarboxylase, Lyase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi4.1.1.12. 5085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase (EC:2.6.1.1, EC:4.1.1.12)
    Alternative name(s):
    Aspartate 4-decarboxylase
    Short name:
    Asd
    Short name:
    AsdP
    Gene namesi
    Name:asD
    OrganismiPseudomonas sp.
    Taxonomic identifieri306 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 693SYM → EEE: Loss of activity. Dissociation into dimers. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylasePRO_0000419124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei314 – 3141N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homododecamer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-48315N.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni13 – 153Combined sources
    Helixi16 – 216Combined sources
    Helixi28 – 358Combined sources
    Helixi46 – 6318Combined sources
    Helixi82 – 9110Combined sources
    Turni92 – 954Combined sources
    Helixi97 – 11115Combined sources
    Helixi117 – 12913Combined sources
    Beta strandi135 – 1384Combined sources
    Helixi141 – 15414Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi169 – 1713Combined sources
    Helixi172 – 18716Combined sources
    Beta strandi195 – 2017Combined sources
    Helixi204 – 2085Combined sources
    Turni213 – 2153Combined sources
    Helixi226 – 2283Combined sources
    Helixi234 – 2374Combined sources
    Helixi238 – 2414Combined sources
    Beta strandi245 – 2539Combined sources
    Turni255 – 2573Combined sources
    Helixi263 – 27513Combined sources
    Beta strandi281 – 2855Combined sources
    Helixi287 – 2893Combined sources
    Beta strandi292 – 2943Combined sources
    Helixi298 – 3014Combined sources
    Turni303 – 3053Combined sources
    Beta strandi306 – 3116Combined sources
    Turni312 – 3165Combined sources
    Helixi319 – 3213Combined sources
    Beta strandi324 – 3318Combined sources
    Helixi333 – 3375Combined sources
    Helixi343 – 35210Combined sources
    Turni353 – 3564Combined sources
    Helixi365 – 3739Combined sources
    Turni374 – 3785Combined sources
    Helixi379 – 3813Combined sources
    Helixi386 – 40015Combined sources
    Helixi406 – 42318Combined sources
    Turni424 – 4274Combined sources
    Beta strandi439 – 4446Combined sources
    Helixi445 – 4528Combined sources
    Helixi455 – 46410Combined sources
    Helixi467 – 47711Combined sources
    Beta strandi494 – 4985Combined sources
    Helixi504 – 52724Combined sources
    Turni528 – 5314Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZY2X-ray3.30A1-531[»]
    ProteinModelPortaliQ53IZ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53IZ1.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR022518. Aspartate_4-decarboxylase.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 2 hits.
    TIGRFAMsiTIGR03801. asp_4_decarbox. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q53IZ1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKDYRSLAN LSPFELKDEL IKVASGKANR LMLNAGRGNP NFLATTPRRA
    60 70 80 90 100
    FFRLGLFAAA ESELSYSYMT VGVGGLAKLD GIEGRFERFI AEHRDQEGVK
    110 120 130 140 150
    FLGKSLSYVR DQLGLDPAAF LHEMVDGILG CNYPVPPRML TVSEQIVRQY
    160 170 180 190 200
    IVREMAGGAV PPESVDLFAV EGGTAAMAYI FESLRISGLL KAGDKVAIGM
    210 220 230 240 250
    PVFTPYIEIP ELAQYDLKEV PIHADPDNGW QYSDAELDKL KDPDVKIFFC
    260 270 280 290 300
    VNPSNPPSVK MDQRSLDRVR AIVAEQRPDL LILTDDVYGT FADEFQSLFS
    310 320 330 340 350
    VCPRNTLLVY SFSKYFGATG WRLGVIAAHK DNVFDHALSQ LPESAKKALD
    360 370 380 390 400
    HRYRSLLPDV RSLKFIDRLV ADSRVVALNH TAGLSTPQQV QMVLFSLFAL
    410 420 430 440 450
    MDEADAYKQA LKQLIRRREA TLYRELGMPP LENPNSVNYY TLIDLQNVTC
    460 470 480 490 500
    RLYGEAFSQW AVQQSSTGDM LFRVADETGI VLLPGRGFGS DRPSGRASLA
    510 520 530
    NLNEYEYAAI GRALRRLADE LYEQYKALGK E
    Length:531
    Mass (Da):59,246
    Last modified:May 24, 2005 - v1
    Checksum:iC2EE19A83CC7B00D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF506011 Genomic DNA. Translation: AAQ07948.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF506011 Genomic DNA. Translation: AAQ07948.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZY2X-ray3.30A1-531[»]
    ProteinModelPortaliQ53IZ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48315N.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi4.1.1.12. 5085.

    Miscellaneous databases

    EvolutionaryTraceiQ53IZ1.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR022518. Aspartate_4-decarboxylase.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 2 hits.
    TIGRFAMsiTIGR03801. asp_4_decarbox. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiASDP_PSESP
    AccessioniPrimary (citable) accession number: Q53IZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: May 24, 2005
    Last modified: April 1, 2015
    This is version 50 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

    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.