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Protein

ADP-L-glycero-D-manno-heptose-6-epimerase

Gene

hldD

Organism
Escherichia coli (strain K12)
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 interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.2 Publications

Miscellaneous

Essential for E.coli viability at elevated temperatures. Insertional inactivation of the gene by the Tn5 transposon results in E.coli being unable to form colonies at temperatures above 43 degrees Celsius.

Caution

Was originally thought to be a homohexamer.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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

NADP+2 Publications, NAD+2 PublicationsNote: Binds 1 NADP+ per subunit. NAD+ can substitute for NADP+, but enzymatic activity is reduced.2 Publications

<p>This subsection of the ‘Function’ 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

Completely inhibited by ADP and ADP-glucose, and partially inhibited by ATP and NADH.

<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=0.1 mM for ADP-heptose1 Publication
  1. Vmax=1.53 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 5.5-9.5.1 Publication

Temperature dependencei

Optimum temperature is 42 degrees Celsius.1 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: ADP-L-glycero-beta-D-manno-heptose biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Bifunctional protein HldE (hldE)
  2. D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (gmhB)
  3. Bifunctional protein HldE (hldE)
  4. ADP-L-glycero-D-manno-heptose-6-epimerase (hldD)
This subpathway is part of the pathway ADP-L-glycero-beta-D-manno-heptose 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 ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate, the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

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 sitei38NADP1 Publication1
Binding sitei53NADP1 Publication1
Binding sitei92NADP1 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 sitei140Proton acceptor1 Publication1
Binding sitei144NADP1 Publication1
Binding sitei169Substrate1 Publication1
Binding sitei170NADP; via amide nitrogen1 Publication1
Active sitei178Proton acceptor1 Publication1
Binding sitei178NADP1 Publication1
Binding sitei180Substrate; via carbonyl oxygen1 Publication1
Binding sitei187Substrate1 Publication1
Binding sitei209Substrate1 Publication1
Binding sitei272Substrate1 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 – 11NADP1 Publication2
Nucleotide bindingi31 – 32NADP1 Publication2
Nucleotide bindingi75 – 79NADP1 Publication5

<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

  • ADP-glyceromanno-heptose 6-epimerase activity Source: EcoCyc
  • NADP+ binding Source: EcoCyc

GO - Biological processi

  • ADP-L-glycero-beta-D-manno-heptose biosynthetic process Source: UniProtKB-UniPathway
  • lipopolysaccharide core region biosynthetic process Source: EcoCyc

<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 functionIsomerase
Biological processCarbohydrate metabolism, Lipopolysaccharide biosynthesis, Stress response
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10838-MONOMER
MetaCyc:EG10838-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.1.3.20 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P67910

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

More...
UniPathwayi
UPA00356;UER00440

UPA00958

<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:
ADP-L-glycero-D-manno-heptose-6-epimerase (EC:5.1.3.201 Publication)
Alternative name(s):
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Short name:
ADP-glyceromanno-heptose 6-epimerase
Short name:
ADP-hep 6-epimerase
Short name:
AGME
<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:hldD
Synonyms:htrM, rfaD, waaD
Ordered Locus Names:b3619, JW3594
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10838 hldD

<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>Mutagenesisi140Y → F: Severely compromises epimerase activitie. 1 Publication1
Mutagenesisi178K → M: Severely compromises epimerase activitie. 1 Publication1
Mutagenesisi208K → M: Activity similar to that of the wild-type. 1 Publication1
Mutagenesisi210D → N: Activity similar to that of the wild-type. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB01774 Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester

<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_00002057931 – 310ADP-L-glycero-D-manno-heptose-6-epimeraseAdd BLAST310

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 residuei267N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P67910

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P67910

PRoteomics IDEntifications database

More...
PRIDEi
P67910

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P67910

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P67910

<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

By heat shock.

<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

Homopentamer.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4263293, 559 interactors

Database of interacting proteins

More...
DIPi
DIP-35958N

Protein interaction database and analysis system

More...
IntActi
P67910, 40 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3801

<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

1310
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P67910

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

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SMRi
P67910

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P67910

<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>Regioni201 – 204Substrate binding1 Publication4

<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

Contains a large N-terminal NADP-binding domain associated with a modified Rossman fold, and a smaller C-terminal substrate-binding domain.

<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
ENOG4105CUI Bacteria
COG0451 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000167987

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P67910

KEGG Orthology (KO)

More...
KOi
K03274

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P67910

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05248 ADP_GME_SDR_e, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01601 Heptose_epimerase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001509 Epimerase_deHydtase
IPR011912 Heptose_epim
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01370 Epimerase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02197 heptose_epim, 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.

P67910-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIIVTGGAGF IGSNIVKALN DKGITDILVV DNLKDGTKFV NLVDLNIADY
60 70 80 90 100
MDKEDFLIQI MAGEEFGDVE AIFHEGACSS TTEWDGKYMM DNNYQYSKEL
110 120 130 140 150
LHYCLEREIP FLYASSAATY GGRTSDFIES REYEKPLNVY GYSKFLFDEY
160 170 180 190 200
VRQILPEANS QIVGFRYFNV YGPREGHKGS MASVAFHLNT QLNNGESPKL
210 220 230 240 250
FEGSENFKRD FVYVGDVADV NLWFLENGVS GIFNLGTGRA ESFQAVADAT
260 270 280 290 300
LAYHKKGQIE YIPFPDKLKG RYQAFTQADL TNLRAAGYDK PFKTVAEGVT
310
EYMAWLNRDA
Length:310
Mass (Da):34,893
Last modified:October 11, 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:i4B9388A879CB7522
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M33577 Genomic DNA Translation: AAA24525.1
X54492 Genomic DNA Translation: CAA38364.1
U00039 Genomic DNA Translation: AAB18596.1
U00096 Genomic DNA Translation: AAC76643.1
AP009048 Genomic DNA Translation: BAE77673.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JU0299

NCBI Reference Sequences

More...
RefSeqi
NP_418076.1, NC_000913.3
WP_000587764.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76643; AAC76643; b3619
BAE77673; BAE77673; BAE77673

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948134

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3594
eco:b3619

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3087

<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
M33577 Genomic DNA Translation: AAA24525.1
X54492 Genomic DNA Translation: CAA38364.1
U00039 Genomic DNA Translation: AAB18596.1
U00096 Genomic DNA Translation: AAC76643.1
AP009048 Genomic DNA Translation: BAE77673.1
PIRiJU0299
RefSeqiNP_418076.1, NC_000913.3
WP_000587764.1, NZ_LN832404.1

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
1EQ2X-ray2.00A/B/C/D/E/F/G/H/I/J1-310[»]
2X6TX-ray2.36A/B/C/D/E/F/G/H/I/J1-310[»]
ProteinModelPortaliP67910
SMRiP67910
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263293, 559 interactors
DIPiDIP-35958N
IntActiP67910, 40 interactors
STRINGi316385.ECDH10B_3801

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB01774 Adenosine-5'-Monophosphate Glucopyranosyl-Monophosphate Ester

PTM databases

iPTMnetiP67910

2D gel databases

SWISS-2DPAGEiP67910

Proteomic databases

EPDiP67910
PaxDbiP67910
PRIDEiP67910

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76643; AAC76643; b3619
BAE77673; BAE77673; BAE77673
GeneIDi948134
KEGGiecj:JW3594
eco:b3619
PATRICifig|1411691.4.peg.3087

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0831
EcoGeneiEG10838 hldD

Phylogenomic databases

eggNOGiENOG4105CUI Bacteria
COG0451 LUCA
HOGENOMiHOG000167987
InParanoidiP67910
KOiK03274
PhylomeDBiP67910

Enzyme and pathway databases

UniPathwayi
UPA00356;UER00440

UPA00958

BioCyciEcoCyc:EG10838-MONOMER
MetaCyc:EG10838-MONOMER
BRENDAi5.1.3.20 2026
SABIO-RKiP67910

Miscellaneous databases

EvolutionaryTraceiP67910

Protein Ontology

More...
PROi
PR:P67910

Family and domain databases

CDDicd05248 ADP_GME_SDR_e, 1 hit
HAMAPiMF_01601 Heptose_epimerase, 1 hit
InterProiView protein in InterPro
IPR001509 Epimerase_deHydtase
IPR011912 Heptose_epim
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF01370 Epimerase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR02197 heptose_epim, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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<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 nameiHLDD_ECOLI
<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: P67910
Secondary accession number(s): P17963, Q2M7T3
<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: October 11, 2004
Last sequence update: October 11, 2004
Last modified: December 5, 2018
This is version 130 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, 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
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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