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Entry version 50 (02 Jun 2021)
Sequence version 1 (13 Jun 2006)
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Protein

Alpha-ketoglutaric semialdehyde dehydrogenase 1

Gene

araE

Organism
Azospirillum brasilense
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 NAD(P)+-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NAD+ to NADP+ as a cosubstrate. Displays broad substrate specificity: exhibits the highest activity with alphaKGSA and succinic semialdehyde as substrates, but to a lesser extent, is also active with glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.

1 Publication

Miscellaneous

A.brasilense possesses two isozymes of alphaKGSA dehydrogenase with essential physiological roles for the L-arabinose and D-glucarate/D-galactarate metabolisms, respectively. The L-arabinose isozyme was isolated in PubMed:16835232 and is described in this entry. The other NAD+-preferring isozyme of alphaKGSA dehydrogenase is induced dramatically by D-glucarate or D-galactarate but not by L-arabinose.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

The catalytic efficiency with alphaKGSA in the presence of NAD+ is 5.2- and 6.2-fold higher than with succinic semialdehyde and glutaraldehyde, respectively. When NADP+ is used as a cosubstrate, the catalytic efficiency with alphaKGSA drops 6-fold compared with that in the presence of NAD+.
  1. KM=11.0 µM for alpha-ketoglutaric semialdehyde (in the presence of NAD+, at 25 degrees Celsius and pH 7.2)1 Publication
  2. KM=15.9 µM for alpha-ketoglutaric semialdehyde (in the presence of NADP+, at 25 degrees Celsius and pH 7.2)1 Publication
  3. KM=38.5 µM for succinic semialdehyde (in the presence of NAD+, at 25 degrees Celsius and pH 7.2)1 Publication
  4. KM=16.3 µM for glutaraldehyde (in the presence of NAD+, at 25 degrees Celsius and pH 7.2)1 Publication
  1. Vmax=42.5 µmol/min/mg enzyme for the oxidation of alpha-ketoglutaric semialdehyde with NAD+ (at 25 degrees Celsius and pH 7.2)1 Publication
  2. Vmax=9.85 µmol/min/mg enzyme for the oxidation of alpha-ketoglutaric semialdehyde with NADP+ (at 25 degrees Celsius and pH 7.2)1 Publication
  3. Vmax=24.7 µmol/min/mg enzyme for the oxidation of succinic semialdehyde with NAD+ (at 25 degrees Celsius and pH 7.2)1 Publication
  4. Vmax=13.9 µmol/min/mg enzyme for the oxidation of glutaraldehyde with NAD+ (at 25 degrees Celsius and pH 7.2)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei253Proton acceptorBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei254NADP; via carbonyl oxygenBy similarity1
Active sitei287NucleophileBy similarity1
Binding sitei384NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi154 – 155NADPBy similarity2
Nucleotide bindingi178 – 181NADPBy similarity4
Nucleotide bindingi231 – 232NADPBy similarity2

<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 processArabinose catabolism, Carbohydrate metabolism
LigandNAD, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.24, 611
1.2.1.26, 611

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q1JUP4

<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%5Fand%5Ftaxonomy%5Fsection">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:
Alpha-ketoglutaric semialdehyde dehydrogenase 1 (EC:1.2.1.261 Publication)
Short name:
alphaKGSA dehydrogenase 1
Alternative name(s):
2,5-dioxovalerate dehydrogenase 1
2-oxoglutarate semialdehyde dehydrogenase 1
KGSADH-ICurated
Succinate-semialdehyde dehydrogenase [NAD(+)] (EC:1.2.1.24)
Short name:
SSDH
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:araE
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiAzospirillum brasilense
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri192 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are unable to grow on L-arabinose as a sole carbon source but grow on a nutrient-rich medium or D-glucose at the same growth rate as the wild-type strain. Moreover, both the wild-type and the mutant strains can grow on D-glucarate or D-galactarate as a sole carbon source.1 Publication

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004185081 – 481Alpha-ketoglutaric semialdehyde dehydrogenase 1Add BLAST481

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by L-arabinose, and to a lesser extent by D-glucose or a nutrient-rich medium.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

<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

1481
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q1JUP4

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016161, Ald_DH/histidinol_DH
IPR016163, Ald_DH_C
IPR016162, Ald_DH_N
IPR015590, Aldehyde_DH_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00171, Aldedh, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53720, SSF53720, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q1JUP4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANVTYTDTQ LLIDGEWVDA ASGKTIDVVN PATGKPIGRV AHAGIADLDR
60 70 80 90 100
ALAAAQSGFE AWRKVPAHER AATMRKAAAL VRERADAIAQ LMTQEQGKPL
110 120 130 140 150
TEARVEVLSA ADIIEWFADE GRRVYGRIVP PRNLGAQQTV VKEPVGPVAA
160 170 180 190 200
FTPWNFPVNQ VVRKLSAALA TGCSFLVKAP EETPASPAAL LRAFVDAGVP
210 220 230 240 250
AGVIGLVYGD PAEISSYLIP HPVIRKVTFT GSTPVGKQLA SLAGLHMKRA
260 270 280 290 300
TMELGGHAPV IVAEDADVAL AVKAAGGAKF RNAGQVCISP TRFLVHNSIR
310 320 330 340 350
DEFTRALVKH AEGLKVGNGL EEGTTLGALA NPRRLTAMAS VIDNARKVGA
360 370 380 390 400
SIETGGERIG SEGNFFAPTV IANVPLDADV FNNEPFGPVA AIRGFDKLEE
410 420 430 440 450
AIAEANRLPF GLAGYAFTRS FANVHLLTQR LEVGMLWINQ PATPWPEMPF
460 470 480
GGVKDSGYGS EGGPEALEPY LVTKSVTVMA V
Length:481
Mass (Da):50,831
Last modified:June 13, 2006 - 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:i9AEFB070DD8D681D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB241137 Genomic DNA Translation: BAE94276.1

<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
AB241137 Genomic DNA Translation: BAE94276.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5X5TX-ray2.25A/B2-481[»]
5X5UX-ray2.30A/B2-481[»]
SMRiQ1JUP4
ModBaseiSearch...
PDBe-KBiSearch...

Enzyme and pathway databases

BRENDAi1.2.1.24, 611
1.2.1.26, 611
SABIO-RKiQ1JUP4

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161, Ald_DH/histidinol_DH
IPR016163, Ald_DH_C
IPR016162, Ald_DH_N
IPR015590, Aldehyde_DH_dom
PfamiView protein in Pfam
PF00171, Aldedh, 1 hit
SUPFAMiSSF53720, SSF53720, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiKGSD1_AZOBR
<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: Q1JUP4
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: June 13, 2006
Last modified: June 2, 2021
This is version 50 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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