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Protein

Alanine dehydrogenase

Gene

ala

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Can not use NADP+ instead of NAD+ as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity.UniRule annotation1 Publication

Catalytic activityi

L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH.UniRule annotation1 Publication

Kineticsi

kcat is 6.1 sec(-1) and 9.6 sec(-1) for the oxidative deamination of L-alanine and L-2-aminobutyrate, respectively (at pH 8.5 and 82 degrees Celsius). kcat is 118 sec(-1), 143 sec(-1) and 113 sec(-1) for the reductive amination of pyruvate, 2-oxobutyrate and oxaloacetate, respectively (at pH 8.5 and 82 degrees Celsius).
  1. KM=0.71 mM for L-alanine (at pH 8.5 and 82 degrees Celsius)1 Publication
  2. KM=0.085 mM for L-2-aminobutyrate (at pH 8.5 and 82 degrees Celsius)1 Publication
  3. KM=0.60 mM for NAD+ (at pH 8.5 and 82 degrees Celsius)1 Publication
  4. KM=0.16 mM for pyruvate (at pH 8.5 and 82 degrees Celsius)1 Publication
  5. KM=0.48 mM for 2-oxobutyrate (at pH 8.5 and 82 degrees Celsius)1 Publication
  6. KM=0.97 mM for oxaloacetate (at pH 8.5 and 82 degrees Celsius)1 Publication
  7. KM=0.02 mM for NADH (at pH 8.5 and 82 degrees Celsius)1 Publication
  8. KM=17.3 mM for NH4+ (at pH 8.5 and 82 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is about 7.0 for both the deamination and amination reactions.1 Publication

    Temperature dependencei

    Optimum temperature is 82 degrees Celsius for the reductive amination of pyruvate. Retains 30% of its maximum activity at 25 degrees Celsius. Completely loses its activity when incubated at 90 degrees Celsius for 2 hours. The thermostability of the enzyme is increased by more than 10-fold by 1.5 M KCl to a half-life of 55 hours at 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei65Proton donor/acceptor1 Publication1
    Binding sitei108NADUniRule annotation1 Publication1
    Binding sitei223NADUniRule annotation1 Publication1
    Binding sitei290NADUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi135 – 136NADUniRule annotation1 Publication2
    Nucleotide bindingi157 – 159NADUniRule annotation1 Publication3
    Nucleotide bindingi217 – 219NADUniRule annotation1 Publication3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    LigandNAD, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi1.4.1.1 414

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine dehydrogenaseUniRule annotation (EC:1.4.1.1UniRule annotation)
    Short name:
    AlaDHUniRule annotation
    Gene namesi
    Name:alaUniRule annotation
    Ordered Locus Names:AF_1665
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    Proteomesi
    • UP000002199 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004216821 – 322Alanine dehydrogenaseAdd BLAST322

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    STRINGi224325.AF1665

    Structurei

    Secondary structure

    1322
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliO28608
    SMRiO28608
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO28608

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ornithine cyclodeaminase/mu-crystallin family. Archaeal alanine dehydrogenase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG01035 Archaea
    COG2423 LUCA
    KOiK19244
    OMAiHTHINAM
    OrthoDBiPOG093Z06G6

    Family and domain databases

    Gene3Di3.30.1780.10, 1 hit
    HAMAPiMF_00935 AlaDH_arch, 1 hit
    InterProiView protein in InterPro
    IPR012742 Ala_DH_archaeglobus
    IPR028609 AlaDH_arch-typ
    IPR036291 NAD(P)-bd_dom_sf
    IPR003462 ODC_Mu_crystall
    IPR023401 ODC_N
    PANTHERiPTHR13812 PTHR13812, 1 hit
    PfamiView protein in Pfam
    PF02423 OCD_Mu_crystall, 1 hit
    PIRSFiPIRSF001439 CryM, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR02371 ala_DH_arch, 1 hit

    Sequencei

    Sequence statusi: Complete.

    O28608-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    METLILTQEE VESLISMDEA MNAVEEAFRL YALGKAQMPP KVYLEFEKGD
    60 70 80 90 100
    LRAMPAHLMG YAGLKWVNSH PGNPDKGLPT VMALMILNSP ETGFPLAVMD
    110 120 130 140 150
    ATYTTSLRTG AAGGIAAKYL ARKNSSVFGF IGCGTQAYFQ LEALRRVFDI
    160 170 180 190 200
    GEVKAYDVRE KAAKKFVSYC EDRGISASVQ PAEEASRCDV LVTTTPSRKP
    210 220 230 240 250
    VVKAEWVEEG THINAIGADG PGKQELDVEI LKKAKIVVDD LEQAKHGGEI
    260 270 280 290 300
    NVAVSKGVIG VEDVHATIGE VIAGLKDGRE SDEEITIFDS TGLAIQDVAV
    310 320
    AKVVYENALS KNVGSKIKFF RI
    Length:322
    Mass (Da):34,829
    Last modified:January 1, 1998 - v1
    Checksum:iE89F1B5C22326956
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000782 Genomic DNA Translation: AAB89583.1
    PIRiH69457
    RefSeqiWP_010879161.1, NC_000917.1

    Genome annotation databases

    EnsemblBacteriaiAAB89583; AAB89583; AF_1665
    GeneIDi24795408
    KEGGiafu:AF_1665

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000782 Genomic DNA Translation: AAB89583.1
    PIRiH69457
    RefSeqiWP_010879161.1, NC_000917.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1OMOX-ray2.32A/B1-322[»]
    1VLLX-ray2.80A/B1-322[»]
    ProteinModelPortaliO28608
    SMRiO28608
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224325.AF1665

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAB89583; AAB89583; AF_1665
    GeneIDi24795408
    KEGGiafu:AF_1665

    Phylogenomic databases

    eggNOGiarCOG01035 Archaea
    COG2423 LUCA
    KOiK19244
    OMAiHTHINAM
    OrthoDBiPOG093Z06G6

    Enzyme and pathway databases

    BRENDAi1.4.1.1 414

    Miscellaneous databases

    EvolutionaryTraceiO28608

    Family and domain databases

    Gene3Di3.30.1780.10, 1 hit
    HAMAPiMF_00935 AlaDH_arch, 1 hit
    InterProiView protein in InterPro
    IPR012742 Ala_DH_archaeglobus
    IPR028609 AlaDH_arch-typ
    IPR036291 NAD(P)-bd_dom_sf
    IPR003462 ODC_Mu_crystall
    IPR023401 ODC_N
    PANTHERiPTHR13812 PTHR13812, 1 hit
    PfamiView protein in Pfam
    PF02423 OCD_Mu_crystall, 1 hit
    PIRSFiPIRSF001439 CryM, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR02371 ala_DH_arch, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiALADH_ARCFU
    AccessioniPrimary (citable) accession number: O28608
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2013
    Last sequence update: January 1, 1998
    Last modified: November 7, 2018
    This is version 99 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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