[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PE577 / Serotype 2a; PubMed=7507920 [NCBI, ExPASy, EBI, Israel, Japan] Morona R., Mavris M., Fallarino A., Manning P.A.; "Characterization of the rfc region of Shigella flexneri."; J. Bacteriol. 176:733-747(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=301 / Serotype 2a; DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan] Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."; Nucleic Acids Res. 30:4432-4441(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 700930 / 2457T / Serotype 2a; DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan] Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."; Infect. Immun. 71:2775-2786(2003).

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

X71970; CAA50784.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE005674; AAN43628.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP17456.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_707921.1; -.
NP_837647.1; -.

3D structure databases

ModBase

P37793.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN43628.1-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.

ProtoNet

P37793.

Genome annotation databases

GeneID

1025295; -.
1078510; -.

GenomeReviews

AE014073_GR; S2209.
AE005674_GR; SF2088.

KEGG

sfl:SF2088; -.
sfx:S2209; -.

Phylogenomic databases

HOGENOM

P37793; -.

Genome annotation databases

CMR

P37793; SF2088.

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_0000136429`
`REGION`	`1 114`	`114`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`115 203`	`89`	`Phosphoribosyl-ATP pyrophosphohydrolase.`

Sequence information

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

Molecular weight: 22882 Da [This is the MW of the unprocessed precursor]

CRC64: 51EC7BDA1D0BAEC0 [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
LWIKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGNTAH QWLFLYQLEQ 

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

       190        200 
LVLLQDQDLD LTTVIENLHK RHQ

P37793 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