Reviewed, UniProtKB/Swiss-Prot Q6GDD2 (HIS2_STAAR)

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:	SAR2754

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
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 By similarity 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 – 210	210	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136433
Regions
	Region	1 – 106	106	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	107 – 210	104	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q6GDD2-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: EB5AA9395B1DB6D7	FASTA	210	23,973
	10 20 30 40 50 60 MTNYKIDFSK GLVPAILQDN QTKQVLMLGY MNQEAFDKTI EDGVVCFYSR SKQRLWTKGE 70 80 90 100 110 120 TSGHTQRVKD IHVDCDNDTI LIDVIPNGPT CHTGSQSCFN TEVPFSVQTL AQTVQDSAQS 130 140 150 160 170 180 NNEKSYTKYL LTEGIEKITK KYGEEAFEVV IEAIKGDKKA FVSEVADELY HLFVLMHALG 190 200 210 VDFSEIEAEL ARRHHKRNNF KGERQNIEQW

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG41729.1.
RefSeq	YP_042091.1.
3D structure databases
SMR	Q6GDD2. Positions 9-104, 107-196.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GDD2.
Genome annotation databases
GeneID	2860714.
GenomeReviews	Gene locus SAR2754 in contig BX571856_GR.
KEGG	sar:SAR2754.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0139.
HOGENOM	HBG294308.
OMA	VHYWSRS.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR2754-MONOMER.
Family and domain databases
HAMAP	MF_01019. HisIE. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. IPR021130. PRib-ATP_pyroPHydrolase-like. [Graphical view]
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_STAAR

Accession

Primary (citable) accession number: Q6GDD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 33 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)