Reviewed, UniProtKB/Swiss-Prot Q9S5G3 (HIS2_ECO57)

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:	Z3188, ECs2827

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

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

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.

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...

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_0000136413
Regions
	Region	1 – 114	114	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	115 – 203	89	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q9S5G3-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 26F0100EDF4DD60D	FASTA	203	22,841
	10 20 30 40 50 60 MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTIESGK VTFFSRTKQR 70 80 90 100 110 120 LWTKGETSGN FLNVVNIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ 130 140 150 160 170 180 LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL 190 200 LVLLQDQDLD LTTVIENLRK RHQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157." Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y. Microb. Pathog. 26:235-247(1999) [PubMed: 10222209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H- / 184 / EHEC.
[2]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB008676 Genomic DNA. Translation: BAA77739.1. AE005174 Genomic DNA. Translation: AAG57085.1. BA000007 Genomic DNA. Translation: BAB36250.1.
PIR	A85828. C90982.
RefSeq	NP_288531.1. NP_310854.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	912426. 962084.
GenomeReviews	Gene locus Z3188 in contig AE005174_GR. Gene locus ECs2827 in contig BA000007_GR.
KEGG	ece:Z3188. ecs:ECs2827.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9S5G3.
OMA	VHYWSRS.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2827-MON.
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...

Entry information

Entry name

HIS2_ECO57

Accession

Primary (citable) accession number: Q9S5G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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