Histidine biosynthesis bifunctional protein hisIE

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Reviewed, UniProtKB/Swiss-Prot P06989 (HIS2_ECOLI)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisIE
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
                Short name=PRA-CH
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphatase
                Short name=PRA-PH
              EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	b2026, JW2008

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-ATP + H₂O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01019 1-(5-phosphoribosyl)-AMP + H₂O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular location	Cytoplasm. HAMAP MF_01019
Sequence similarities	In the N-terminal section; belongs to the PRA-CH family. In the C-terminal section; belongs to the PRA-PH family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 203

203

Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019

PRO_0000136411

Regions

Region

1 – 114

114

Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019

Region

115 – 203

Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Natural variations

Natural variant

Q → L in strain: F719. HAMAP MF_01019

Natural variant

L → I in strain: F719. HAMAP MF_01019

Natural variant

164

H → N in strain: F719. HAMAP MF_01019

Natural variant

192 – 193

TT → GE in strain: F719. HAMAP MF_01019

Natural variant

196

E → D in strain: F719. HAMAP MF_01019

Natural variant

199 – 200

RK → KN in strain: F719. HAMAP MF_01019

Natural variant

203

Missing in strain: F719. HAMAP MF_01019

Experimental info

Sequence conflict

S → P in CAA31818. Ref.1

Sequence conflict

193

T → P Ref.1

Sequence conflict

193

T → P Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P06989-1 [UniParc].

Last modified February 1, 1995. Version 3.
Checksum: 34019009D82E0122
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FASTA

203

22,756

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3062174] [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: 3018428] [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: 8201624] [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: 7536735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O9:K31-:H- / F719.
[5]	"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." 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. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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Cross-references

Sequence databases
	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.
PIR	YNECHI. JS0135.
RefSeq	AP_002627.1. NP_416530.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9907N.
Genome annotation databases
GeneID	946515.
GenomeReviews	Gene locus JW2008 in contig AP009048_GR. Gene locus b2026 in contig U00096_GR.
KEGG	ecj:JW2008. eco:b2026.
Organism-specific databases
EchoBASE	EB0446.
EcoGene	EG10451. hisI.
CMR	Search...
Phylogenomic databases
HOGENOM	P06989.
OMA	P06989. VHYWSRS.
Enzyme and pathway databases
BioCyc	EcoCyc:HISTCYCLOPRATPPHOS. MetaCyc:HISTCYCLOPRATPPHOS.
Family and domain databases
HAMAP	MF_01019. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view]
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. histidine_hisI. 1 hit.
ProtoNet	Search...

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Entry information

Entry name

HIS2_ECOLI

Accession

Primary (citable) accession number: P06989
Secondary accession number(s): P78079, Q47596

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents