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Entry version 90 (08 May 2019)
Sequence version 1 (21 Dec 2004)
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Protein

UDP-glucose 6-dehydrogenase

Gene

UGDH

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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 formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (By similarity). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity).By similarity

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor. It binds at the same site as the substrate, but functions as allosteric inhibitor by triggering a conformation change that disrupts the active hexameric ring structure and gives rise to an inactive, horseshoe-shaped hexamer.By similarity

<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: UDP-alpha-D-glucuronate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. UDP-glucose 6-dehydrogenase (UGDH)
This subpathway is part of the pathway UDP-alpha-D-glucuronate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose, the pathway UDP-alpha-D-glucuronate biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei36NADBy similarity1
Binding sitei41NADBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei161Proton donor/acceptorBy similarity1
Binding sitei165NADBy similarity1
Active sitei220Proton donor/acceptorBy similarity1
Binding sitei260SubstrateBy similarity1
Active sitei276NucleophileBy similarity1
Binding sitei346NADBy similarity1
Binding sitei442SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi11 – 16NADBy similarity6
Nucleotide bindingi89 – 93NADBy similarity5
Nucleotide bindingi130 – 132NADBy similarity3
Nucleotide bindingi276 – 279NADBy 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

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 functionAllosteric enzyme, Oxidoreductase
Biological processCarbohydrate metabolism
LigandNAD

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00038;UER00491

<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:
UDP-glucose 6-dehydrogenase (EC:1.1.1.22By similarity)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
<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:UGDH
<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>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<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 identifieri9601 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
<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
  • UP000001595 <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: Unplaced

<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_00003174771 – 494UDP-glucose 6-dehydrogenaseAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei107N6-acetyllysineBy similarity1
Modified residuei476PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q5R7B3

<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

Homohexamer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9601.ENSPPYP00000016396

<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

3D structure databases

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

More...
SMRi
Q5R7B3

Database of comparative protein structure models

More...
ModBasei
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni88 – 110Intrinsically disordered; important for formation of active hexamer structureBy similarityAdd BLAST23
Regioni129 – 135Allosteric switch regionBy similarity7
Regioni161 – 165Substrate bindingBy similarity5
Regioni220 – 224Substrate bindingBy similarity5
Regioni267 – 273Substrate bindingBy similarity7
Regioni321 – 325Important for formation of active hexamer structureBy similarity5
Regioni338 – 339Substrate bindingBy similarity2
Regioni466 – 494Intrinsically disorderedBy similarityAdd BLAST29

<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

The protein goes through several conformation states during the reaction cycle, giving rise to hysteresis. In the initial state, the ligand-free protein is in an inactive conformation (E*). Substrate binding triggers a change to the active conformation (E). UDP-xylose binding triggers the transition to a distinct, inhibited conformation. The presence of an intrinsically disordered C-terminus promotes a more dynamic protein structure and favors a conformation with high affinity for UPD-xylose.By similarity
The allosteric switch region moves by about 5 Angstroms when UDP-xylose is bound, and occupies part of the UDP-glucose binding site. At the same time it promotes domain movements that disrupt the active hexameric ring structure and lead to the formation of a horseshoe-shaped, inactive hexamer.By similarity

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2666 Eukaryota
COG1004 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000153773

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5R7B3

KEGG Orthology (KO)

More...
KOi
K00012

Database of Orthologous Groups

More...
OrthoDBi
915490at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR036291 NAD(P)-bd_dom_sf
IPR017476 UDP-Glc/GDP-Man
IPR014027 UDP-Glc/GDP-Man_DH_C
IPR036220 UDP-Glc/GDP-Man_DH_C_sf
IPR014026 UDP-Glc/GDP-Man_DH_dimer
IPR001732 UDP-Glc/GDP-Man_DH_N
IPR028356 UDPglc_DH_euk

The PANTHER Classification System

More...
PANTHERi
PTHR11374 PTHR11374, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00984 UDPG_MGDP_dh, 1 hit
PF03720 UDPG_MGDP_dh_C, 1 hit
PF03721 UDPG_MGDP_dh_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500133 UDPglc_DH_euk, 1 hit
PIRSF000124 UDPglc_GDPman_dh, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00984 UDPG_MGDP_dh_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit
SSF52413 SSF52413, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03026 NDP-sugDHase, 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>. 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_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.

Q5R7B3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFEIKKICCI GAGYVGGPTC SVIAHMRPEI RVTVVDVNES RINAWNSPTL
60 70 80 90 100
PIYEPGLKEV VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK
110 120 130 140 150
GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP
160 170 180 190 200
NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQR AVQALCAVYE
210 220 230 240 250
HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE
260 270 280 290 300
VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW
310 320 330 340 350
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS
360 370 380 390 400
IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD
410 420 430 440 450
PYEACDGAHA VVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHN
460 470 480 490
ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP KFSLQDPPNK KPKV
Length:494
Mass (Da):55,077
Last modified:December 21, 2004 - 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:i9584347DAD728943
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
CR860205 mRNA Translation: CAH92347.1

NCBI Reference Sequences

More...
RefSeqi
NP_001127543.1, NM_001134071.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100174620

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pon:100174620

<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
CR860205 mRNA Translation: CAH92347.1
RefSeqiNP_001127543.1, NM_001134071.1

3D structure databases

SMRiQ5R7B3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000016396

Proteomic databases

PRIDEiQ5R7B3

Genome annotation databases

GeneIDi100174620
KEGGipon:100174620

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7358

Phylogenomic databases

eggNOGiKOG2666 Eukaryota
COG1004 LUCA
HOGENOMiHOG000153773
InParanoidiQ5R7B3
KOiK00012
OrthoDBi915490at2759

Enzyme and pathway databases

UniPathwayiUPA00038;UER00491

Family and domain databases

InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR036291 NAD(P)-bd_dom_sf
IPR017476 UDP-Glc/GDP-Man
IPR014027 UDP-Glc/GDP-Man_DH_C
IPR036220 UDP-Glc/GDP-Man_DH_C_sf
IPR014026 UDP-Glc/GDP-Man_DH_dimer
IPR001732 UDP-Glc/GDP-Man_DH_N
IPR028356 UDPglc_DH_euk
PANTHERiPTHR11374 PTHR11374, 1 hit
PfamiView protein in Pfam
PF00984 UDPG_MGDP_dh, 1 hit
PF03720 UDPG_MGDP_dh_C, 1 hit
PF03721 UDPG_MGDP_dh_N, 1 hit
PIRSFiPIRSF500133 UDPglc_DH_euk, 1 hit
PIRSF000124 UDPglc_GDPman_dh, 1 hit
SMARTiView protein in SMART
SM00984 UDPG_MGDP_dh_C, 1 hit
SUPFAMiSSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit
SSF52413 SSF52413, 1 hit
TIGRFAMsiTIGR03026 NDP-sugDHase, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiUGDH_PONAB
<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: Q5R7B3
<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: February 5, 2008
Last sequence update: December 21, 2004
Last modified: May 8, 2019
This is version 90 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 programChordata 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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