NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

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 (By similarity).
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

BA000033; BAB96456.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_647408.1; -.

3D structure databases

ModBase

Q8NUI4.

Enzyme and pathway databases

BioCyc

SAUR196620:MW2591-MON; -.

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

1004727; -.

GenomeReviews

BA000033_GR; MW2591.

KEGG

sam:MW2591; -.

Phylogenomic databases

HOGENOM

Q8NUI4; -.

Genome annotation databases

CMR

Q8NUI4; MW2591.

Other

ProtoNet

Q8NUI4.

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`	`1 210`	`210`	`Histidine biosynthesis bifunctional protein hisIE.`	`PRO_0000136435`
`REGION`	`1 106`	`106`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`107 210`	`104`	`Phosphoribosyl-ATP pyrophosphohydrolase.`

Sequence information

Length: 210 AA [This is the length of the unprocessed precursor]

Molecular weight: 23973 Da [This is the MW of the unprocessed precursor]

CRC64: EB5AA9395B1DB6D7 [This is a checksum on the sequence]

        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

Q8NUI4 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