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Protein

Histidine biosynthesis bifunctional protein HisB

Gene

hisB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei9NucleophileUniRule annotation1
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

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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 databases

ChEMBLiCHEMBL2366452

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001582061 – 355Histidine biosynthesis bifunctional protein HisBAdd BLAST355

Proteomic databases

EPDiP06987
PaxDbiP06987
PRIDEiP06987

2D gel databases

SWISS-2DPAGEiP06987

Interactioni

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260405, 19 interactors
DIPiDIP-9901N
IntActiP06987, 5 interactors
STRINGi316385.ECDH10B_2170

Structurei

3D structure databases

ProteinModelPortaliP06987
SMRiP06987
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 166Histidinol-phosphataseUniRule annotationAdd BLAST166
Regioni167 – 355Imidazoleglycerol-phosphate dehydrataseUniRule annotationAdd BLAST189

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
PhylomeDBiP06987

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

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
PATRICifig|1411691.4.peg.230

Similar proteinsi

Entry informationi

Entry nameiHIS7_ECOLI
AccessioniPrimary (citable) accession number: P06987
Secondary accession number(s): P78077
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 28, 2018
This is version 157 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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