[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/BF00422061; PubMed=3018428 [NCBI, ExPASy, EBI, Israel, Japan] Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.; "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region."; Mol. Gen. Genet. 203:382-388(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=K12; DOI=10.1006/jmbi.1994.1384; PubMed=8201624 [NCBI, ExPASy, EBI, Israel, Japan] Jovanovic G., Kostic T., Jankovic M., Savic D.J.; "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited."; J. Mol. Biol. 239:433-435(1994).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=O9:K31-:H- / F719; PubMed=7536735 [NCBI, ExPASy, EBI, Israel, Japan] Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T., Kato N., Jann K.; "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."; J. Bacteriol. 177:2178-2187(1995).
[5]	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).
[6]	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).
[7]	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: 1-(5-phosphoribosyl)-ATP + H₂O = 1-(5-phosphoribosyl)-AMP + diphosphate.
CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H₂O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9 .
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9 .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
SIMILARITY: In the C-terminal section; belongs to the PRA-PH 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

X13462; CAA31818.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03974; CAA27613.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U02072; AAA19744.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D43637; BAA07753.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75087.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15858.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JS0135; YNECHI.

RefSeq

AP_002627.1; -.
NP_416530.1; -.

3D structure databases

ModBase

P06989.

Protein-protein interaction databases

DIP

DIP:9907N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:HISTCYCLOPRATPPHOS; -.
MetaCyc:HISTCYCLOPRATPPHOS; -.

Organism-specific databases

EchoBASE

EB0446; -.

EcoGene

EG10451; hisI.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004635;	Molecular function: phosphoribosyl-AMP cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004636;	Molecular function: phosphoribosyl-ATP diphosphatase 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_01019; -; 1.
PBIL [Tree]

InterPro

IPR002496; PRA_CycOHase.
IPR008179; PRib-ATP_pyrophosphohydrolase.
Graphical view of domain structure.

Pfam

PF01502; PRA-CH; 1.
PF01503; PRA-PH; 1.
Pfam graphical view of domain structure.

ProDom

PD002610; PRA_cyclohydro; 1.
PD002611; Pra_PH/CH; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03188; histidine_hisI; 1.

Genome annotation databases

GeneID

946515; -.

GenomeReviews

U00096_GR; b2026.
AP009048_GR; JW2008.

KEGG

ecj:JW2008; -.
eco:b2026; -.

Phylogenomic databases

HOGENOM

P06989; -.

Genome annotation databases

CMR

P06989; b2026.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 203`	`203`	`Histidine biosynthesis bifunctional protein hisIE.`	`PRO_0000136411`
`REGION`	`1 114`	`114`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`115 203`	`89`	`Phosphoribosyl-ATP pyrophosphohydrolase.`
`VARIANT`	`5 5`	`1`	`Q -> L (in strain: F719).`
`VARIANT`	`46 46`	`1`	`L -> I (in strain: F719).`
`VARIANT`	`164 164`	`1`	`H -> N (in strain: F719).`
`VARIANT`	`192 193`	`2`	`TT -> GE (in strain: F719).`
`VARIANT`	`196 196`	`1`	`E -> D (in strain: F719).`
`VARIANT`	`199 200`	`2`	`RK -> KN (in strain: F719).`
`VARIANT`	`203 203`	`1`	`Missing (in strain: F719).`
`CONFLICT`	`68 68`		`S -> P (in Ref. 1; CAA31818).`
`CONFLICT`	`193 193`		`T -> P (in Ref. 1 and 2).`

Sequence information

Length: 203 AA [This is the length of the unprocessed precursor]

Molecular weight: 22756 Da [This is the MW of the unprocessed precursor]

CRC64: 34019009D82E0122 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTLESGK VTFFSRTKQR 

        70         80         90        100        110        120 
LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ 

       130        140        150        160        170        180 
LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL 

       190        200 
LVLLQDQGLD LTTVIENLRK RHQ

P06989 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