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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.24 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.15 mM for NADP+1 Publication
  3. KM=1.6 mM for phosphate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via DAP pathway

    This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
    4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
    This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

    Pathwayi: L-methionine biosynthesis via de novo pathway

    This protein is involved in step 2 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

    Pathwayi: L-threonine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
    4. Homoserine kinase (thrB)
    5. Threonine synthase (thrC)
    This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei74NADP1 Publication1
    Binding sitei103Phosphate1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei136Acyl-thioester intermediate2 Publications1
    Binding sitei163Substrate1 Publication1
    Binding sitei166NADP; via carbonyl oxygen1 Publication1
    Binding sitei243Substrate1 Publication1
    Binding sitei246Phosphate1 Publication1
    Binding sitei270Substrate1 Publication1
    Active sitei277Proton acceptor1 Publication1
    Binding sitei353NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 13NADP1 Publication4
    Nucleotide bindingi37 – 38NADP1 Publication2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    HINF71421:G1GJ1-681-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.1.11 2529

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00034;UER00016

    UPA00050;UER00463

    UPA00051;UER00464

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenaseUniRule annotation (EC:1.2.1.112 Publications)
    Short name:
    ASA dehydrogenaseUniRule annotation
    Short name:
    ASADHUniRule annotation
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenaseUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:asdUniRule annotation
    Ordered Locus Names:HI_0646
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri71421 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000579 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi103R → K: 2-fold increase in affinity for ASA, 23-fold decrease in affinity for phosphate, and 275-fold decrease in activity. 1 Publication1
    Mutagenesisi103R → L: 7-fold increase in affinity for ASA, 150-fold decrease in affinity for phosphate, and 1400-fold decrease in activity. 1 Publication1
    Mutagenesisi243E → D: No change in affinity for ASA and 82-fold decrease in activity. 1 Publication1
    Mutagenesisi246K → R: 2-fold increase in affinity for ASA, nearly no change in affinity for phosphate, and 30-fold decrease in activity. 1 Publication1
    Mutagenesisi270R → K: 2-fold decrease in affinity for ASA and 825-fold decrease in activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03502 (4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB04498 Aspartate Semialdehyde

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001413751 – 371Aspartate-semialdehyde dehydrogenaseAdd BLAST371

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P44801

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    71421.HI0646

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1371
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NWCX-ray2.04A/B1-371[»]
    1NWHX-ray2.00A/B1-371[»]
    1NX6X-ray2.15A1-371[»]
    1OZAX-ray2.06A1-371[»]
    1PQPX-ray2.06A1-371[»]
    1PQUX-ray1.92A/B/C/D1-371[»]
    1PR3X-ray2.15A1-371[»]
    1PS8X-ray2.40A1-371[»]
    1PU2X-ray2.06A1-371[»]
    1Q2XX-ray2.05A/B1-371[»]
    1TA4X-ray2.28A1-371[»]
    1TB4X-ray2.15A1-371[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P44801

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P44801

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P44801

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain.1 Publication

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CM3 Bacteria
    COG0136 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K00133

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VGTDPTW

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P44801

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02121 ASADH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000319 Asp-semialdehyde_DH_CS
    IPR011534 Asp_ADH_gamma-type
    IPR012080 Asp_semialdehyde_DH
    IPR036291 NAD(P)-bd_dom_sf
    IPR000534 Semialdehyde_DH_NAD-bd
    IPR012280 Semialdhyde_DH_dimer_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10174:SF116 PTHR10174:SF116, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01118 Semialdhyde_dh, 1 hit
    PF02774 Semialdhyde_dhC, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00859 Semialdhyde_dh, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01745 asd_gamma, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01103 ASD, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P44801-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKNVGFIGWR GMVGSVLMDR MSQENDFENL NPVFFTTSQA GQKAPVFGGK
    60 70 80 90 100
    DAGDLKSAFD IEELKKLDII VTCQGGDYTN EVYPKLKATG WDGYWVDAAS
    110 120 130 140 150
    ALRMKDDAII VLDPVNQHVI SEGLKKGIKT FVGGNCTVSL MLMAIGGLFE
    160 170 180 190 200
    KDLVEWISVA TYQAASGAGA KNMRELLSQM GLLEQAVSSE LKDPASSILD
    210 220 230 240 250
    IERKVTAKMR ADNFPTDNFG AALGGSLIPW IDKLLPETGQ TKEEWKGYAE
    260 270 280 290 300
    TNKILGLSDN PIPVDGLCVR IGALRCHSQA FTIKLKKDLP LEEIEQIIAS
    310 320 330 340 350
    HNEWVKVIPN DKEITLRELT PAKVTGTLSV PVGRLRKLAM GPEYLAAFTV
    360 370
    GDQLLWGAAE PVRRILKQLV A
    Length:371
    Mass (Da):40,539
    Last modified:November 1, 1995 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE44CE5B90F2AF041
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    L42023 Genomic DNA Translation: AAC22306.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B64084

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_438806.1, NC_000907.1
    WP_005694497.1, NC_000907.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC22306; AAC22306; HI_0646

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    949960

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hin:HI0646

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|71421.8.peg.675

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42023 Genomic DNA Translation: AAC22306.1
    PIRiB64084
    RefSeqiNP_438806.1, NC_000907.1
    WP_005694497.1, NC_000907.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NWCX-ray2.04A/B1-371[»]
    1NWHX-ray2.00A/B1-371[»]
    1NX6X-ray2.15A1-371[»]
    1OZAX-ray2.06A1-371[»]
    1PQPX-ray2.06A1-371[»]
    1PQUX-ray1.92A/B/C/D1-371[»]
    1PR3X-ray2.15A1-371[»]
    1PS8X-ray2.40A1-371[»]
    1PU2X-ray2.06A1-371[»]
    1Q2XX-ray2.05A/B1-371[»]
    1TA4X-ray2.28A1-371[»]
    1TB4X-ray2.15A1-371[»]
    ProteinModelPortaliP44801
    SMRiP44801
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi71421.HI0646

    Chemistry databases

    DrugBankiDB03502 (4s)-4-{[(2s)-2-Amino-3-Oxopropyl]Sulfanyl}-L-Homoserinate
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB04498 Aspartate Semialdehyde

    Proteomic databases

    PRIDEiP44801

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC22306; AAC22306; HI_0646
    GeneIDi949960
    KEGGihin:HI0646
    PATRICifig|71421.8.peg.675

    Phylogenomic databases

    eggNOGiENOG4105CM3 Bacteria
    COG0136 LUCA
    KOiK00133
    OMAiVGTDPTW
    PhylomeDBiP44801

    Enzyme and pathway databases

    UniPathwayi
    UPA00034;UER00016

    UPA00050;UER00463

    UPA00051;UER00464

    BioCyciHINF71421:G1GJ1-681-MONOMER
    BRENDAi1.2.1.11 2529

    Miscellaneous databases

    EvolutionaryTraceiP44801

    Family and domain databases

    HAMAPiMF_02121 ASADH, 1 hit
    InterProiView protein in InterPro
    IPR000319 Asp-semialdehyde_DH_CS
    IPR011534 Asp_ADH_gamma-type
    IPR012080 Asp_semialdehyde_DH
    IPR036291 NAD(P)-bd_dom_sf
    IPR000534 Semialdehyde_DH_NAD-bd
    IPR012280 Semialdhyde_DH_dimer_dom
    PANTHERiPTHR10174:SF116 PTHR10174:SF116, 1 hit
    PfamiView protein in Pfam
    PF01118 Semialdhyde_dh, 1 hit
    PF02774 Semialdhyde_dhC, 1 hit
    SMARTiView protein in SMART
    SM00859 Semialdhyde_dh, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01745 asd_gamma, 1 hit
    PROSITEiView protein in PROSITE
    PS01103 ASD, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHAS_HAEIN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P44801
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: December 5, 2018
    This is version 134 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
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