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Protein

Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase

Gene

asD

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
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.2 Publications

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=9 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 sitei115 – 1151Aspartate; via amide nitrogenBy similarity
    Binding sitei256 – 2561AspartateBy similarity
    Binding sitei497 – 4971AspartateBy 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

    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:
    AsdA
    Gene namesi
    Name:asD
    OrganismiComamonas testosteroni (Pseudomonas testosteroni)
    Taxonomic identifieri285 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

    Pathology & Biotechi

    Biotechnological usei

    Is highly specific for L-aspartic acid, and so can be used to produce L-alanine and D-aspartic acid from DL-aspartic acid.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi134 – 1341Y → F: Slightly reduced activity. 1 Publication
    Mutagenesisi315 – 3151K → A: Slightly reduced activity. 1 Publication
    Mutagenesisi487 – 4871R → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylasePRO_0000419123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei315 – 3151N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homododecamer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-48316N.
    STRINGi399795.CtesDRAFT_PD2303.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64Combined sources
    Helixi13 – 2311Combined sources
    Helixi27 – 359Combined sources
    Beta strandi41 – 444Combined sources
    Helixi46 – 6318Combined sources
    Beta strandi74 – 763Combined sources
    Helixi83 – 9311Combined sources
    Turni94 – 963Combined sources
    Helixi98 – 11215Combined sources
    Helixi118 – 13013Combined sources
    Beta strandi136 – 1394Combined sources
    Helixi142 – 15514Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi166 – 1727Combined sources
    Helixi173 – 18715Combined sources
    Beta strandi196 – 2027Combined sources
    Helixi205 – 2128Combined sources
    Turni214 – 2163Combined sources
    Beta strandi219 – 2246Combined sources
    Helixi227 – 2293Combined sources
    Helixi235 – 2384Combined sources
    Helixi239 – 2424Combined sources
    Beta strandi246 – 2549Combined sources
    Beta strandi256 – 2583Combined sources
    Helixi264 – 27613Combined sources
    Beta strandi282 – 2865Combined sources
    Helixi290 – 2923Combined sources
    Beta strandi293 – 2953Combined sources
    Helixi299 – 3024Combined sources
    Helixi304 – 3063Combined sources
    Beta strandi307 – 3137Combined sources
    Turni314 – 3185Combined sources
    Helixi320 – 3223Combined sources
    Beta strandi324 – 3329Combined sources
    Helixi334 – 3407Combined sources
    Helixi344 – 35411Combined sources
    Turni355 – 3573Combined sources
    Helixi361 – 3633Combined sources
    Helixi366 – 3738Combined sources
    Turni374 – 3796Combined sources
    Helixi380 – 3823Combined sources
    Helixi387 – 40216Combined sources
    Helixi407 – 42418Combined sources
    Helixi425 – 4273Combined sources
    Beta strandi440 – 4456Combined sources
    Helixi446 – 4549Combined sources
    Helixi456 – 46510Combined sources
    Helixi468 – 47912Combined sources
    Beta strandi484 – 4874Combined sources
    Beta strandi495 – 5039Combined sources
    Helixi505 – 52521Combined sources
    Helixi529 – 5335Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZY3X-ray2.50A/B/C/D/E/F1-533[»]
    2ZY4X-ray2.00A/B/C/D/E/F1-533[»]
    2ZY5X-ray2.65A/B/C/D/E/F1-533[»]
    ProteinModelPortaliQ93QX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93QX0.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CEB. Bacteria.
    COG0436. LUCA.

    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.

    Q93QX0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKDYQSLAK LSPFELKDEL IKIASSDGNR LMLNAGRGNP NFLATTPRRA
    60 70 80 90 100
    FFRLGLFAAA ESELSYSYMT TVGVGGLAKI DGIEGRFERY IAENRDQEGV
    110 120 130 140 150
    RFLGKSLSYV RDQLGLDPAA FLHEMVDGIL GCNYPVPPRM LNISEKIVRQ
    160 170 180 190 200
    YIIREMGADA IPSESVNLFA VEGGTAAMAY IFESLKLNGL LKAGDKVAIG
    210 220 230 240 250
    MPVFTPYIEI PELAQYALEE VAINADPSLN WQYPDSELDK LKDPAIKIFF
    260 270 280 290 300
    CVNPSNPPSV KMDQRSLERV RNIVAEHRPD LMILTDDVYG TFADDFQSLF
    310 320 330 340 350
    AICPENTLLV YSFSKYFGAT GWRLGVVAAH QQNVFDLALD KLQESEKVAL
    360 370 380 390 400
    DHRYRSLLPD VRSLKFIDRL VADSRAVALN HTAGLSTPQQ VQMALFSLFA
    410 420 430 440 450
    LMDEADEYKH TLKQLIRRRE TTLYRELGMP PLRDENAVDY YTLIDLQDVT
    460 470 480 490 500
    AKLYGEAFSE WAVKQSSTGD MLFRIADETG IVLLPGRGFG SNRPSGRASL
    510 520 530
    ANLNEYEYAA IGRALRKMAD ELYAEYSGQA QNL
    Length:533
    Mass (Da):59,584
    Last modified:December 1, 2001 - v1
    Checksum:iB6E0042383A51113
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF168368 Genomic DNA. Translation: AAK58507.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF168368 Genomic DNA. Translation: AAK58507.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZY3X-ray2.50A/B/C/D/E/F1-533[»]
    2ZY4X-ray2.00A/B/C/D/E/F1-533[»]
    2ZY5X-ray2.65A/B/C/D/E/F1-533[»]
    ProteinModelPortaliQ93QX0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48316N.
    STRINGi399795.CtesDRAFT_PD2303.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4105CEB. Bacteria.
    COG0436. LUCA.

    Miscellaneous databases

    EvolutionaryTraceiQ93QX0.

    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...

    Publicationsi

    1. "Cloning, expression and characterization of L-aspartate - decarboxylase gene from Alcaligenes faecalis CCRC 11585."
      Chen C.-C., Chou T.-L., Lee C.-Y.
      J. Ind. Microbiol. Biotechnol. 25:132-140(2000)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
      Strain: ATCC 25094 / DSM 30032 / N.
    2. "Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase."
      Chen H.J., Ko T.P., Lee C.Y., Wang N.C., Wang A.H.
      Structure 17:517-529(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, MUTAGENESIS OF TYR-134; LYS-315 AND ARG-487.
      Strain: ATCC 25094 / DSM 30032 / N.

    Entry informationi

    Entry nameiASDA_COMTE
    AccessioniPrimary (citable) accession number: Q93QX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: December 1, 2001
    Last modified: November 11, 2015
    This is version 66 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.