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UniProtKB - Q2VEQ7 (DDH_HALMT)

Entry version 63 (16 Jan 2019)
Sequence version 1 (10 Jan 2006)
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Protein

D-2-hydroxyacid dehydrogenase

Gene

ddh

Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
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 stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. Can use both NADPH or NADH as reductant, displaying a marked preference for NADPH over NADH. Shows a broad substrate specificity, although it displays a marked preference for the 2-ketocarboxylic acids having an unbranched chain of 4-5 carbon atoms.1 Publication

<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=1.31 mM for 2-ketoisoleucine (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
  2. KM=11.9 mM for 2-ketoisoleucine (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
  3. KM=3.77 mM for 2-ketoisocaproate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
  4. KM=13.9 mM for 2-ketoisocaproate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
  5. KM=13.45 mM for 2-ketobutyrate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
  6. KM=106 mM for 2-ketobutyrate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
  7. KM=21.96 mM for pyruvate (in the presence of NADPH, at pH 5 and 40 degrees Celsius)1 Publication
  8. KM=0.046 mM for NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
  9. KM=0.33 mM for NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
  1. Vmax=1.733 µmol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
  2. Vmax=1.02 µmol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
  3. Vmax=1.47 µmol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
  4. Vmax=0.94 µmol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
  5. Vmax=2.09 µmol/min/mg enzyme for the reduction of 2-ketobutyrate by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
  6. Vmax=2.1 µmol/min/mg enzyme for the reduction of 2-ketobutyrate by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
  7. Vmax=0.8 µmol/min/mg enzyme for the reduction of pyruvate by NADPH (at pH 5 and 40 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei226By similarity1
<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 sitei250NADBy similarity1
Active sitei255By similarity1
Active sitei274Proton donorBy similarity1

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 bindingi145 – 146NADBy similarity2
Nucleotide bindingi224 – 226NADBy similarity3
Nucleotide bindingi274 – 277NADBy similarity4

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		HMED523841:G1HBL-2706-MONOMER
MetaCyc:MONOMER-17694

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.272 2566

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q2VEQ7

<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:
D-2-hydroxyacid dehydrogenase (EC:1.1.1.-)
Short name:
D2-HDH
Alternative name(s):
D-specific 2-hydroxyacid dehydrogenase
<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:ddh
Synonyms:serA5
Ordered Locus Names:HFX_2024
<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>OrganismiHaloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
<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 identifieri523841 [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 lineageiArchaea › Euryarchaeota › Stenosarchaea group › Halobacteria › Haloferacales › Haloferacaceae › Haloferax ›
<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
  • UP000006469 <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 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_00004144971 – 308D-2-hydroxyacid dehydrogenaseAdd BLAST308

<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

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

1308
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
5MH5X-ray1.40A/B1-308[»]
5MH6X-ray1.35A/B/C/D1-308[»]
5MHAX-ray1.57A/B1-308[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q2VEQ7

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

More...SMRi		Q2VEQ7

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 D-isomer specific 2-hydroxyacid dehydrogenase family.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K17064

Identification of Orthologs from Complete Genome Data

More...OMAi		YGAGVDH

Database of Orthologous Groups

More...OrthoDBi		36410at2157

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006140 D-isomer_DH_NAD-bd
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02826 2-Hacid_dh_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735 SSF51735, 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.

Q2VEQ7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHIERLAVDE SVGRAMPPQR FIEALSDLGV PVEFAGEDEQ FGPGDAVASF 
        60         70         80         90        100
GHRDAFLDAD WVHCIRAGYD EFPVGVYEEA GTYLTNSTGI HGTTVGETVA 
       110        120        130        140        150
GYMLTFARRL HAYRDAQHDH AWDLPRYEEP FTLAGERVCV VGLGTLGRGV 
       160        170        180        190        200
VDRAAALGME VVGVRRSGDP VDNVSTVYTP DRLHEAIADA RFVVLATPLT 
       210        220        230        240        250
DETEGMVAAP EFETMREDAS LVNVARGPVV VESDLVAALD SGDIAGAALD 
       260        270        280        290        300
VFSEEPLPED SPLWDFEDVL ITPHVSAATS KYHEDVAALI RENIEKIATG 

DELTNRVV
Length:308
Mass (Da):33,336
Last modified:January 10, 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:i20D4FB8CE01D64AA
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
DQ223970 Genomic DNA Translation: ABB30004.1
CP001868 Genomic DNA Translation: AFK19716.1

NCBI Reference Sequences

More...RefSeqi		WP_004059362.1, NZ_CP007551.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AFK19716; AFK19716; HFX_2024

Database of genes from NCBI RefSeq genomes

More...GeneIDi		13028184

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hme:HFX_2024

<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
DQ223970 Genomic DNA Translation: ABB30004.1
CP001868 Genomic DNA Translation: AFK19716.1
RefSeqiWP_004059362.1, NZ_CP007551.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MH5X-ray1.40A/B1-308[»]
5MH6X-ray1.35A/B/C/D1-308[»]
5MHAX-ray1.57A/B1-308[»]
ProteinModelPortaliQ2VEQ7
SMRiQ2VEQ7
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFK19716; AFK19716; HFX_2024
GeneIDi13028184
KEGGihme:HFX_2024

Phylogenomic databases

KOiK17064
OMAiYGAGVDH
OrthoDBi36410at2157

Enzyme and pathway databases

BioCyciHMED523841:G1HBL-2706-MONOMER
MetaCyc:MONOMER-17694
BRENDAi1.1.1.272 2566
SABIO-RKiQ2VEQ7

Family and domain databases

InterProiView protein in InterPro
IPR006140 D-isomer_DH_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF02826 2-Hacid_dh_C, 1 hit
SUPFAMiSSF51735 SSF51735, 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 nameiDDH_HALMT
<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: Q2VEQ7
Secondary accession number(s): I3R656
<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: December 14, 2011
Last sequence update: January 10, 2006
Last modified: January 16, 2019
This is version 63 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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