Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alanine dehydrogenase

Gene

ala

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Proton donor/acceptor1 Publication
    Binding sitei108 – 1081NADUniRule annotation1 Publication
    Binding sitei223 – 2231NADUniRule annotation1 Publication
    Binding sitei290 – 2901NADUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi135 – 1362NADUniRule annotation1 Publication
    Nucleotide bindingi157 – 1593NADUniRule annotation1 Publication
    Nucleotide bindingi217 – 2193NADUniRule annotation1 Publication

    GO - Molecular functioni

    • alanine dehydrogenase activity Source: UniProtKB
    • NAD binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-1699-MONOMER.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Alanine dehydrogenasePRO_0000421682Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    STRINGi224325.AF1665.

    Structurei

    Secondary structure

    1
    322
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Helixi8 – 125Combined sources
    Helixi17 – 3216Combined sources
    Beta strandi42 – 454Combined sources
    Beta strandi50 – 589Combined sources
    Beta strandi61 – 699Combined sources
    Turni71 – 733Combined sources
    Helixi74 – 763Combined sources
    Beta strandi83 – 886Combined sources
    Turni90 – 923Combined sources
    Beta strandi95 – 1006Combined sources
    Helixi102 – 12019Combined sources
    Beta strandi127 – 1315Combined sources
    Helixi135 – 14713Combined sources
    Beta strandi152 – 1565Combined sources
    Helixi160 – 17213Combined sources
    Beta strandi177 – 1793Combined sources
    Helixi182 – 1854Combined sources
    Beta strandi187 – 1937Combined sources
    Helixi204 – 2063Combined sources
    Beta strandi212 – 2154Combined sources
    Helixi228 – 2325Combined sources
    Beta strandi234 – 2396Combined sources
    Helixi241 – 2477Combined sources
    Helixi251 – 2555Combined sources
    Helixi261 – 2633Combined sources
    Beta strandi264 – 2674Combined sources
    Helixi268 – 2725Combined sources
    Beta strandi285 – 2895Combined sources
    Helixi294 – 31118Combined sources
    Beta strandi314 – 3174Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OMOX-ray2.32A/B1-322[»]
    1VLLX-ray2.80A/B1-322[»]
    ProteinModelPortaliO28608.
    SMRiO28608. Positions 1-321.
    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.
    OMAiKVYVDCY.

    Family and domain databases

    Gene3Di3.30.1780.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_00935. AlaDH_arch. 1 hit.
    InterProiIPR012742. Ala_DH_archaeglobus.
    IPR028609. AlaDH_arch-typ.
    IPR016040. NAD(P)-bd_dom.
    IPR003462. ODC_Mu_crystall.
    IPR023401. ODC_N.
    [Graphical view]
    PfamiPF02423. OCD_Mu_crystall. 1 hit.
    [Graphical view]
    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.

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OMOX-ray2.32A/B1-322[»]
    1VLLX-ray2.80A/B1-322[»]
    ProteinModelPortaliO28608.
    SMRiO28608. Positions 1-321.
    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.
    OMAiKVYVDCY.

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-1699-MONOMER.
    BRENDAi1.4.1.1. 414.

    Miscellaneous databases

    EvolutionaryTraceiO28608.

    Family and domain databases

    Gene3Di3.30.1780.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_00935. AlaDH_arch. 1 hit.
    InterProiIPR012742. Ala_DH_archaeglobus.
    IPR028609. AlaDH_arch-typ.
    IPR016040. NAD(P)-bd_dom.
    IPR003462. ODC_Mu_crystall.
    IPR023401. ODC_N.
    [Graphical view]
    PfamiPF02423. OCD_Mu_crystall. 1 hit.
    [Graphical view]
    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 historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2013
    Last sequence update: January 1, 1998
    Last modified: September 7, 2016
    This is version 89 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.