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Protein

Histidine biosynthesis bifunctional protein HisIE

Gene

hisI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.

Pathwayi: L-histidine biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
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.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • phosphoribosyl-AMP cyclohydrolase activity Source: EcoCyc
  • phosphoribosyl-ATP diphosphatase activity Source: EcoCyc

GO - Biological processi

  • histidine biosynthetic process Source: EcoCyc

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:HISTCYCLOPRATPPHOS.
ECOL316407:JW2008-MONOMER.
MetaCyc:HISTCYCLOPRATPPHOS.
UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine biosynthesis bifunctional protein HisIE
Including the following 2 domains:
Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
Short name:
PRA-CH
Phosphoribosyl-ATP pyrophosphatase (EC:3.6.1.31)
Short name:
PRA-PH
Gene namesi
Name:hisI
Synonyms:hisIE
Ordered Locus Names:b2026, JW2008
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10451. hisI.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Histidine biosynthesis bifunctional protein HisIEPRO_0000136411Add
BLAST

Proteomic databases

PaxDbiP06989.

Interactioni

Protein-protein interaction databases

BioGridi4260421. 3 interactions.
DIPiDIP-9907N.
IntActiP06989. 15 interactions.
STRINGi511145.b2026.

Structurei

3D structure databases

ProteinModelPortaliP06989.
SMRiP06989. Positions 16-105, 115-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 114114Phosphoribosyl-AMP cyclohydrolaseAdd
BLAST
Regioni115 – 20389Phosphoribosyl-ATP pyrophosphohydrolaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the PRA-CH family.Curated
In the C-terminal section; belongs to the PRA-PH family.Curated

Phylogenomic databases

eggNOGiENOG4105K8F. Bacteria.
COG0139. LUCA.
COG0140. LUCA.
HOGENOMiHOG000277503.
InParanoidiP06989.
KOiK11755.
OMAiERSCFHQ.
OrthoDBiEOG6PGKB6.
PhylomeDBiP06989.

Family and domain databases

HAMAPiMF_01019. HisIE.
MF_01020. HisE.
InterProiIPR023019. His_synth_HisIE.
IPR008179. HisE.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.

Sequencei

Sequence statusi: Complete.

P06989-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTLESGK
60 70 80 90 100
VTFFSRTKQR LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG
110 120 130 140 150
TSSCFGDTAH QWLFLYQLEQ LLAERKSADP ETSYTAKLYA SGTKRIAQKV
160 170 180 190 200
GEEGVETALA ATVHDRFELT NEASDLMYHL LVLLQDQGLD LTTVIENLRK

RHQ
Length:203
Mass (Da):22,756
Last modified:February 1, 1995 - v3
Checksum:i34019009D82E0122
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681S → P in CAA31818 (PubMed:3062174).Curated
Sequence conflicti193 – 1931T → P (PubMed:3062174).Curated
Sequence conflicti193 – 1931T → P (PubMed:3018428).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51Q → L in strain: F719.
Natural varianti46 – 461L → I in strain: F719.
Natural varianti164 – 1641H → N in strain: F719.
Natural varianti192 – 1932TT → GE in strain: F719.
Natural varianti196 – 1961E → D in strain: F719.
Natural varianti199 – 2002RK → KN in strain: F719.
Natural varianti203 – 2031Missing in strain: F719.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31818.1.
X03974 Genomic DNA. Translation: CAA27613.1.
U02072 Unassigned DNA. Translation: AAA19744.1.
D43637 Genomic DNA. Translation: BAA07753.1.
U00096 Genomic DNA. Translation: AAC75087.1.
AP009048 Genomic DNA. Translation: BAA15858.1.
PIRiJS0135. YNECHI.
RefSeqiNP_416530.1. NC_000913.3.
WP_000954911.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75087; AAC75087; b2026.
BAA15858; BAA15858; BAA15858.
GeneIDi946515.
KEGGiecj:JW2008.
eco:b2026.
PATRICi32119387. VBIEscCol129921_2103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31818.1.
X03974 Genomic DNA. Translation: CAA27613.1.
U02072 Unassigned DNA. Translation: AAA19744.1.
D43637 Genomic DNA. Translation: BAA07753.1.
U00096 Genomic DNA. Translation: AAC75087.1.
AP009048 Genomic DNA. Translation: BAA15858.1.
PIRiJS0135. YNECHI.
RefSeqiNP_416530.1. NC_000913.3.
WP_000954911.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP06989.
SMRiP06989. Positions 16-105, 115-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260421. 3 interactions.
DIPiDIP-9907N.
IntActiP06989. 15 interactions.
STRINGi511145.b2026.

Proteomic databases

PaxDbiP06989.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75087; AAC75087; b2026.
BAA15858; BAA15858; BAA15858.
GeneIDi946515.
KEGGiecj:JW2008.
eco:b2026.
PATRICi32119387. VBIEscCol129921_2103.

Organism-specific databases

EchoBASEiEB0446.
EcoGeneiEG10451. hisI.

Phylogenomic databases

eggNOGiENOG4105K8F. Bacteria.
COG0139. LUCA.
COG0140. LUCA.
HOGENOMiHOG000277503.
InParanoidiP06989.
KOiK11755.
OMAiERSCFHQ.
OrthoDBiEOG6PGKB6.
PhylomeDBiP06989.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
BioCyciEcoCyc:HISTCYCLOPRATPPHOS.
ECOL316407:JW2008-MONOMER.
MetaCyc:HISTCYCLOPRATPPHOS.

Miscellaneous databases

PROiP06989.

Family and domain databases

HAMAPiMF_01019. HisIE.
MF_01020. HisE.
InterProiIPR023019. His_synth_HisIE.
IPR008179. HisE.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03188. histidine_hisI. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
    Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
    J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region."
    Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.
    Mol. Gen. Genet. 203:382-388(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited."
    Jovanovic G., Kostic T., Jankovic M., Savic D.J.
    J. Mol. Biol. 239:433-435(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12.
  4. "Expression of the O9 polysaccharide of Escherichia coli: sequencing of the E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and evidence for an ATP-binding cassette transport system."
    Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T., Kato N., Jann K.
    J. Bacteriol. 177:2178-2187(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O9:K31-:H- / F719.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiHIS2_ECOLI
AccessioniPrimary (citable) accession number: P06989
Secondary accession number(s): P78079, Q47596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.