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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-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.UniRule annotation
L-histidinol phosphate + H2O = L-histidinol + phosphate.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • Zn2+UniRule annotation

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)
  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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91NucleophileUniRule annotation
Metal bindingi9 – 91MagnesiumUniRule annotation
Active sitei11 – 111Proton donorUniRule annotation
Metal bindingi11 – 111Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi93 – 931ZincUniRule annotation
Metal bindingi95 – 951Zinc; via pros nitrogenUniRule annotation
Metal bindingi101 – 1011ZincUniRule annotation
Metal bindingi103 – 1031ZincUniRule annotation
Metal bindingi130 – 1301MagnesiumUniRule annotation

GO - Molecular functioni

  • histidinol-phosphatase activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • imidazoleglycerol-phosphate dehydratase activity Source: UniProtKB-HAMAP
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywords - Molecular functioni

Hydrolase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

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
Gene namesi
Name:hisBUniRule annotation
Ordered Locus Names:b2022, JW2004
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10445. hisB.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Histidine biosynthesis bifunctional protein HisBPRO_0000158206Add
BLAST

Proteomic databases

EPDiP06987.
PaxDbiP06987.
PRIDEiP06987.

2D gel databases

SWISS-2DPAGEP06987.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1126930,EBI-1126930
gstBP0ACA74EBI-1126930,EBI-1120568

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260405. 12 interactions.
DIPiDIP-9901N.
IntActiP06987. 5 interactions.
STRINGi511145.b2022.

Structurei

3D structure databases

ProteinModelPortaliP06987.
SMRiP06987. Positions 3-165, 167-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 166166Histidinol-phosphataseUniRule annotationAdd
BLAST
Regioni167 – 355189Imidazoleglycerol-phosphate dehydrataseUniRule annotationAdd
BLAST

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

eggNOGiENOG4105ECC. Bacteria.
COG0131. LUCA.
COG0241. LUCA.
HOGENOMiHOG000228065.
InParanoidiP06987.
KOiK01089.
OMAiPEDTFWP.
OrthoDBiEOG60PHGP.
PhylomeDBiP06987.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_00076. HisB.
MF_01022. Bifunc_HisB.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR020566. His_synth_bifunc_HisB.
IPR005954. HisB_N.
IPR006543. Histidinol-phos.
IPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR013954. PNK3P.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 2 hits.
PfamiPF00475. IGPD. 1 hit.
PF08645. PNK3P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01261. hisB_Nterm. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i5EC09FB68AE40A9D
GO

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.

Genome annotation databases

EnsemblBacteriaiAAC75083; AAC75083; b2022.
BAA15853; BAA15853; BAA15853.
GeneIDi946552.
KEGGiecj:JW2004.
eco:b2022.
PATRICi32119379. VBIEscCol129921_2099.

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

ProteinModelPortaliP06987.
SMRiP06987. Positions 3-165, 167-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260405. 12 interactions.
DIPiDIP-9901N.
IntActiP06987. 5 interactions.
STRINGi511145.b2022.

Chemistry

ChEMBLiCHEMBL2366452.

2D gel databases

SWISS-2DPAGEP06987.

Proteomic databases

EPDiP06987.
PaxDbiP06987.
PRIDEiP06987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75083; AAC75083; b2022.
BAA15853; BAA15853; BAA15853.
GeneIDi946552.
KEGGiecj:JW2004.
eco:b2022.
PATRICi32119379. VBIEscCol129921_2099.

Organism-specific databases

EchoBASEiEB0440.
EcoGeneiEG10445. hisB.

Phylogenomic databases

eggNOGiENOG4105ECC. Bacteria.
COG0131. LUCA.
COG0241. LUCA.
HOGENOMiHOG000228065.
InParanoidiP06987.
KOiK01089.
OMAiPEDTFWP.
OrthoDBiEOG60PHGP.
PhylomeDBiP06987.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP06987.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_00076. HisB.
MF_01022. Bifunc_HisB.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR020566. His_synth_bifunc_HisB.
IPR005954. HisB_N.
IPR006543. Histidinol-phos.
IPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR013954. PNK3P.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 2 hits.
PfamiPF00475. IGPD. 1 hit.
PF08645. PNK3P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01261. hisB_Nterm. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]
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. "Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene."
    Chiariotti L., Nappo A.G., Carlomagno M.S., Bruni C.B.
    Mol. Gen. Genet. 202:42-47(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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 nameiHIS7_ECOLI
AccessioniPrimary (citable) accession number: P06987
Secondary accession number(s): P78077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 6, 2016
This is version 144 of the entry and version 1 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.