[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1016/0022-2836(88)90194-5; PubMed=3062174 [NCBI, ExPASy, EBI, Israel, Japan] Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.; "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."; J. Mol. Biol. 203:585-606(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00330514; PubMed=3007936 [NCBI, ExPASy, EBI, Israel, Japan] Chiariotti L., Nappo A.G., Carlomagno M.S., Bruni C.B.; "Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene."; Mol. Gen. Genet. 202:42-47(1986).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan] Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.; "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."; DNA Res. 3:379-392(1996).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H₂O.
CATALYTIC ACTIVITY: L-histidinol phosphate + H₂O = L-histidinol + phosphate.
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9 .
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9 .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: In the N-terminal section; belongs to the histidinol-phosphatase family.
SIMILARITY: In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03416; CAA27151.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13462; CAA31814.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75083.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15853.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E64967; DWECHB.

RefSeq

AP_002623.1; -.
NP_416526.4; -.

3D structure databases

SMR

P06987; 3-165.

ModBase

P06987.

Enzyme and pathway databases

BioCyc

EcoCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MON; -.
MetaCyc:IMIDPHOSPHADEHYDHISTIDPHOSPHA-MON; -.

2D gel databases

SWISS-2DPAGE

P06987; -.

Organism-specific databases

EchoBASE

EB0440; -.

EcoGene

EG10445; hisB.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004401;	Molecular function: histidinol-phosphatase activity (inferred from electronic annotation from HAMAP).
GO:0004424;	Molecular function: imidazoleglycerol-phosphate dehydratase activity (inferred from electronic annotation from HAMAP).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01022; -; 1.
PBIL [Tree]

InterPro

IPR006549; HAD-SF_hydro_IIIA.
IPR005954; HisB_N.
IPR006543; Histidinol-phos.
IPR000807; Imidazole_glycer-P_deHydtase.
IPR013954; PNK3P_central-region.
Graphical view of domain structure.

PANTHER

PTHR23133:SF2; Imidazole-GPD; 1.

Pfam

PF00475; IGPD; 1.
PF08645; PNK3P; 1.
Pfam graphical view of domain structure.

ProDom

PD002282; IGPD; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01662; HAD-SF-IIIA; 1.
TIGR01261; hisB_Nterm; 1.
TIGR01656; Histidinol-ppas; 1.

PROSITE

PS00954; IGP_DEHYDRATASE_1; 1.
PS00955; IGP_DEHYDRATASE_2; 1.

Genome annotation databases

GeneID

946552; -.

GenomeReviews

U00096_GR; b2022.
AP009048_GR; JW2004.

KEGG

ecj:JW2004; -.
eco:b2022; -.

Phylogenomic databases

HOGENOM

P06987; -.

Genome annotation databases

CMR

P06987; b2022.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 355`	`355`	`Histidine biosynthesis bifunctional protein hisB.`	`PRO_0000158206`
`REGION`	`1 166`	`166`	`Histidinol-phosphatase.`
`REGION`	`167 355`	`189`	`Imidazoleglycerol-phosphate dehydratase.`

Sequence information

Length: 355 AA [This is the length of the unprocessed precursor]

Molecular weight: 40278 Da [This is the MW of the unprocessed precursor]

CRC64: 5EC09FB68AE40A9D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPEL LKLQKAGYKL VMITNQDGLG 

        70         80         90        100        110        120 
TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE CDCRKPKVKL VERYLAEQAM 

       130        140        150        160        170        180 
DRANSYVIGD RATDIQLAEN MGITGLRYDR ETLNWPMIGE QLTRRDRYAH VVRNTKETQI 

       190        200        210        220        230        240 
DVQVWLDREG GSKINTGVGF FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG 

       250        260        270        280        290        300 
EALKIALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH 

       310        320        330        340        350 
FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL

P06987 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools