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Entry version 168 (13 Nov 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Histidine biosynthesis bifunctional protein HisB

Gene

hisB

Organism
Escherichia coli (strain K12)
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 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

<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

Protein has several cofactor binding sites:

<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 6 and 8 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), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB), Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD), 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei9NucleophileUniRule annotation1
<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 bindingi9MagnesiumUniRule annotation1
Active sitei11Proton donorUniRule annotation1
Metal bindingi11Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi93ZincUniRule annotation1
Metal bindingi95Zinc; via pros nitrogenUniRule annotation1
Metal bindingi101ZincUniRule annotation1
Metal bindingi103ZincUniRule annotation1
Metal bindingi130MagnesiumUniRule annotation1

<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 functionHydrolase, Lyase, Multifunctional enzyme
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER
ECOL316407:JW2004-MONOMER
MetaCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER

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

More...
UniPathwayi
UPA00031;UER00011
UPA00031;UER00013

<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:
Histidine biosynthesis bifunctional protein HisBUniRule annotation
Including the following 2 domains:
Histidinol-phosphataseUniRule annotation (EC:3.1.3.15UniRule annotation)
Imidazoleglycerol-phosphate dehydrataseUniRule annotation (EC:4.2.1.19UniRule annotation)
Short name:
IGPDUniRule 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:hisBUniRule annotation
Ordered Locus Names:b2022, JW2004
<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

<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

Keywords - Cellular componenti

Cytoplasm

<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
CHEMBL2366452

<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_00001582061 – 355Histidine biosynthesis bifunctional protein HisBAdd BLAST355

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P06987

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P06987

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

More...
PaxDbi
P06987

PRoteomics IDEntifications database

More...
PRIDEi
P06987

2D gel databases

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

More...
SWISS-2DPAGEi
P06987

<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%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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260405, 19 interactors
850899, 3 interactors

Database of interacting proteins

More...
DIPi
DIP-9901N

Protein interaction database and analysis system

More...
IntActi
P06987, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2022

<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
P06987

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>Regioni1 – 166Histidinol-phosphataseUniRule annotationAdd BLAST166
Regioni167 – 355Imidazoleglycerol-phosphate dehydrataseUniRule annotationAdd BLAST189

<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

In the N-terminal section; belongs to the histidinol-phosphatase family.UniRule annotation
In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105ECC Bacteria
COG0131 LUCA
COG0241 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000228065

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06987

KEGG Orthology (KO)

More...
KOi
K01089

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P06987

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07914 IGPD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.40, 2 hits
3.40.50.1000, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01022 Bifunc_HisB, 1 hit
MF_00076 HisB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036412 HAD-like_sf
IPR006549 HAD-SF_hydro_IIIA
IPR023214 HAD_sf
IPR020566 His_synth_bifunc_HisB
IPR005954 HisB_N
IPR006543 Histidinol-phos
IPR038494 IGPD_sf
IPR000807 ImidazoleglycerolP_deHydtase
IPR020565 ImidazoleglycerP_deHydtase_CS
IPR013954 PNK3P
IPR020568 Ribosomal_S5_D2-typ_fold

The PANTHER Classification System

More...
PANTHERi
PTHR23133 PTHR23133, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00475 IGPD, 1 hit
PF08645 PNK3P, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 2 hits
SSF56784 SSF56784, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01662 HAD-SF-IIIA, 1 hit
TIGR01261 hisB_Nterm, 1 hit
TIGR01656 Histidinol-ppas, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00954 IGP_DEHYDRATASE_1, 1 hit
PS00955 IGP_DEHYDRATASE_2, 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.

P06987-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPEL LKLQKAGYKL
60 70 80 90 100
VMITNQDGLG TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE
110 120 130 140 150
CDCRKPKVKL VERYLAEQAM DRANSYVIGD RATDIQLAEN MGITGLRYDR
160 170 180 190 200
ETLNWPMIGE QLTRRDRYAH VVRNTKETQI DVQVWLDREG GSKINTGVGF
210 220 230 240 250
FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG EALKIALGDK
260 270 280 290 300
RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH
310 320 330 340 350
FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS

SKGVL
Length:355
Mass (Da):40,278
Last modified:April 1, 1988 - 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:i5EC09FB68AE40A9D
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
X03416 Genomic DNA Translation: CAA27151.1
X13462 Genomic DNA Translation: CAA31814.1
U00096 Genomic DNA Translation: AAC75083.2
AP009048 Genomic DNA Translation: BAA15853.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E64967 DWECHB

NCBI Reference Sequences

More...
RefSeqi
NP_416526.4, NC_000913.3
WP_000080105.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75083; AAC75083; b2022
BAA15853; BAA15853; BAA15853

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946552

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2004
eco:b2022

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.230

<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
X03416 Genomic DNA Translation: CAA27151.1
X13462 Genomic DNA Translation: CAA31814.1
U00096 Genomic DNA Translation: AAC75083.2
AP009048 Genomic DNA Translation: BAA15853.1
PIRiE64967 DWECHB
RefSeqiNP_416526.4, NC_000913.3
WP_000080105.1, NZ_LN832404.1

3D structure databases

SMRiP06987
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4260405, 19 interactors
850899, 3 interactors
DIPiDIP-9901N
IntActiP06987, 5 interactors
STRINGi511145.b2022

Chemistry databases

ChEMBLiCHEMBL2366452

2D gel databases

SWISS-2DPAGEiP06987

Proteomic databases

EPDiP06987
jPOSTiP06987
PaxDbiP06987
PRIDEiP06987

Genome annotation databases

EnsemblBacteriaiAAC75083; AAC75083; b2022
BAA15853; BAA15853; BAA15853
GeneIDi946552
KEGGiecj:JW2004
eco:b2022
PATRICifig|1411691.4.peg.230

Organism-specific databases

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

More...
EchoBASEi
EB0440

Phylogenomic databases

eggNOGiENOG4105ECC Bacteria
COG0131 LUCA
COG0241 LUCA
HOGENOMiHOG000228065
InParanoidiP06987
KOiK01089
PhylomeDBiP06987

Enzyme and pathway databases

UniPathwayiUPA00031;UER00011
UPA00031;UER00013
BioCyciEcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER
ECOL316407:JW2004-MONOMER
MetaCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P06987

Family and domain databases

CDDicd07914 IGPD, 1 hit
Gene3Di3.30.230.40, 2 hits
3.40.50.1000, 1 hit
HAMAPiMF_01022 Bifunc_HisB, 1 hit
MF_00076 HisB, 1 hit
InterProiView protein in InterPro
IPR036412 HAD-like_sf
IPR006549 HAD-SF_hydro_IIIA
IPR023214 HAD_sf
IPR020566 His_synth_bifunc_HisB
IPR005954 HisB_N
IPR006543 Histidinol-phos
IPR038494 IGPD_sf
IPR000807 ImidazoleglycerolP_deHydtase
IPR020565 ImidazoleglycerP_deHydtase_CS
IPR013954 PNK3P
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR23133 PTHR23133, 1 hit
PfamiView protein in Pfam
PF00475 IGPD, 1 hit
PF08645 PNK3P, 1 hit
SUPFAMiSSF54211 SSF54211, 2 hits
SSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR01662 HAD-SF-IIIA, 1 hit
TIGR01261 hisB_Nterm, 1 hit
TIGR01656 Histidinol-ppas, 1 hit
PROSITEiView protein in PROSITE
PS00954 IGP_DEHYDRATASE_1, 1 hit
PS00955 IGP_DEHYDRATASE_2, 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 nameiHIS7_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: P06987
Secondary accession number(s): P78077
<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: April 1, 1988
Last modified: November 13, 2019
This is version 168 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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