NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
DOI=10.1101/gr.219302; PubMed=11997336 [NCBI, ExPASy, EBI, Israel, Japan]
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., Wang J., Yu J., Yang H.;
"A complete sequence of the T. tengcongensis genome.";
Genome Res. 12:689-700(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

AE013160; AAM25297.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_623693.1; -.

3D structure databases

ModBase

Q8R886.

Enzyme and pathway databases

BioCyc

TTEN273068:TTE2132-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

Q8R886.

Genome annotation databases

GeneID

997442; -.

GenomeReviews

AE008691_GR; TTE2132.

KEGG

tte:TTE2132; -.

NMPDR

fig|273068.3.peg.2236; -.

Phylogenomic databases

HOGENOM

Q8R886; -.

Genome annotation databases

CMR

Q8R886; TTE2132.

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`	`1 205`	`205`	`Histidine biosynthesis bifunctional protein hisIE.`	`PRO_0000136444`
`REGION`	`1 115`	`115`	`Phosphoribosyl-AMP cyclohydrolase.`
`REGION`	`116 205`	`90`	`Phosphoribosyl-ATP pyrophosphohydrolase.`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 23864 Da [This is the MW of the unprocessed precursor]

CRC64: E2DAFD6A8C5BD65A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIDIKELKFD EKGLIPAIVQ DYYTKQVLML AYMNEESLKL TLEKGETYFF SRSRGKIWHK 

        70         80         90        100        110        120 
GETSGNTQKV KKIFYDCDED ALLIQVEAKG PACHTGNISC FYRSFDEETE DGIEILNKLY 

       130        140        150        160        170        180 
ERIKGRKINP VEGSYTNYLF EKGIDKILKK VGEEATEVVI ASKNDSKDEI VYEVSDLIYH 

       190        200 
LMVLLVEKNI TLNDIYNELE RRYKK

Q8R886 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