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Entry version 176 (08 May 2019)
Sequence version 5 (23 Jan 2007)
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Protein

Histidinol dehydrogenase

Gene

hisD

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 sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

<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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.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: L-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid 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 sitei130NAD1 Publication1
Binding sitei188NAD1 Publication1
Binding sitei211NAD1 Publication1
Binding sitei237Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi259Zinc1 Publication1
Binding sitei259Substrate1 Publication1
Metal bindingi262Zinc1 Publication1
Binding sitei262Substrate1 Publication1
<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 sitei326Proton acceptor1 Publication1
Active sitei327Proton acceptor1 Publication1
Binding sitei327Substrate1 Publication1
Metal bindingi360Zinc1 Publication1
Binding sitei360Substrate1 Publication1
Binding sitei414Substrate1 Publication1
Metal bindingi419Zinc1 Publication1
Binding sitei419Substrate1 Publication1

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

GO - Biological processi

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

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:HISTDEHYD-MONOMER
ECOL316407:JW2002-MONOMER
MetaCyc:HISTDEHYD-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.23 2026

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

More...
UniPathwayi
UPA00031;UER00014

<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:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hisD1 PublicationUniRule annotation
Ordered Locus Names:b2020, JW2002
<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
EG10447 hisD

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2366464

Drug and drug target database

More...
DrugBanki
DB04077 Glycerol
DB03811 Histidinol

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001357702 – 434Histidinol dehydrogenaseAdd BLAST433

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P06988

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P06988

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

More...
PaxDbi
P06988

PRoteomics IDEntifications database

More...
PRIDEi
P06988

2D gel databases

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

More...
SWISS-2DPAGEi
P06988

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

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

Homodimer.UniRule annotation

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260403, 27 interactors

Protein interaction database and analysis system

More...
IntActi
P06988, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2020

<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

1434
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

More...
SMRi
P06988

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P06988

<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 histidinol dehydrogenase family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CEK Bacteria
COG0141 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000243914

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06988

KEGG Orthology (KO)

More...
KOi
K00013

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P06988

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06572 Histidinol_dh, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01024 HisD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR001692 Histidinol_DH_CS
IPR022695 Histidinol_DH_monofunct
IPR012131 Hstdl_DH

The PANTHER Classification System

More...
PANTHERi
PTHR21256 PTHR21256, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00815 Histidinol_dh, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000099 Histidinol_dh, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00083 HOLDHDRGNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53720 SSF53720, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00069 hisD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00611 HISOL_DEHYDROGENASE, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06988-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA
60 70 80 90 100
LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT
110 120 130 140 150
AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAS
160 170 180 190 200
IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV
210 220 230 240 250
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD
260 270 280 290 300
FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ
310 320 330 340 350
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL
360 370 380 390 400
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF
410 420 430
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA
Length:434
Mass (Da):46,110
Last modified:January 23, 2007 - v5
<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:i4B4F2EA00C9BEA4E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti15E → V (PubMed:3062174).Curated1
Sequence conflicti15E → V (PubMed:3018428).Curated1
Sequence conflicti22M → T in CAA27610 (PubMed:3018428).Curated1
Sequence conflicti150S → R (PubMed:3062174).Curated1
Sequence conflicti150S → R (PubMed:3018428).Curated1
Sequence conflicti157V → A in CAA36882 (PubMed:2194167).Curated1
Sequence conflicti313L → S (PubMed:3062174).Curated1
Sequence conflicti313L → S (PubMed:3018428).Curated1
Sequence conflicti403L → V (PubMed:3062174).Curated1
Sequence conflicti403L → V (PubMed:3018428).Curated1

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
X13462 Genomic DNA Translation: CAA31812.1
X03972 Genomic DNA Translation: CAA27610.1
X52656 Genomic DNA Translation: CAA36882.1
U00096 Genomic DNA Translation: AAC75081.1
AP009048 Genomic DNA Translation: BAA15851.1
M10483 Genomic DNA Translation: AAA23962.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C64967 DEECHT

NCBI Reference Sequences

More...
RefSeqi
NP_416524.1, NC_000913.3
WP_000009594.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75081; AAC75081; b2020
BAA15851; BAA15851; BAA15851

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946531

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2002
eco:b2020

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.232

<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
X13462 Genomic DNA Translation: CAA31812.1
X03972 Genomic DNA Translation: CAA27610.1
X52656 Genomic DNA Translation: CAA36882.1
U00096 Genomic DNA Translation: AAC75081.1
AP009048 Genomic DNA Translation: BAA15851.1
M10483 Genomic DNA Translation: AAA23962.1
PIRiC64967 DEECHT
RefSeqiNP_416524.1, NC_000913.3
WP_000009594.1, 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
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
SMRiP06988
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260403, 27 interactors
IntActiP06988, 7 interactors
STRINGi511145.b2020

Chemistry databases

ChEMBLiCHEMBL2366464
DrugBankiDB04077 Glycerol
DB03811 Histidinol

2D gel databases

SWISS-2DPAGEiP06988

Proteomic databases

EPDiP06988
jPOSTiP06988
PaxDbiP06988
PRIDEiP06988

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75081; AAC75081; b2020
BAA15851; BAA15851; BAA15851
GeneIDi946531
KEGGiecj:JW2002
eco:b2020
PATRICifig|1411691.4.peg.232

Organism-specific databases

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

More...
EchoBASEi
EB0442
EcoGeneiEG10447 hisD

Phylogenomic databases

eggNOGiENOG4105CEK Bacteria
COG0141 LUCA
HOGENOMiHOG000243914
InParanoidiP06988
KOiK00013
PhylomeDBiP06988

Enzyme and pathway databases

UniPathwayiUPA00031;UER00014
BioCyciEcoCyc:HISTDEHYD-MONOMER
ECOL316407:JW2002-MONOMER
MetaCyc:HISTDEHYD-MONOMER
BRENDAi1.1.1.23 2026

Miscellaneous databases

EvolutionaryTraceiP06988

Protein Ontology

More...
PROi
PR:P06988

Family and domain databases

CDDicd06572 Histidinol_dh, 1 hit
HAMAPiMF_01024 HisD, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR001692 Histidinol_DH_CS
IPR022695 Histidinol_DH_monofunct
IPR012131 Hstdl_DH
PANTHERiPTHR21256 PTHR21256, 1 hit
PfamiView protein in Pfam
PF00815 Histidinol_dh, 1 hit
PIRSFiPIRSF000099 Histidinol_dh, 1 hit
PRINTSiPR00083 HOLDHDRGNASE
SUPFAMiSSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR00069 hisD, 1 hit
PROSITEiView protein in PROSITE
PS00611 HISOL_DEHYDROGENASE, 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 nameiHISX_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: P06988
Secondary accession number(s): O08506, P78076, Q47254
<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: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 176 of the entry and version 5 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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