UniProtKB - Q81G00 (HIS2_BACCR)
Protein
Phosphoribosyl-ATP pyrophosphatase
Gene
hisE
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Functioni
Catalytic activityi
- 1-(5-phospho-β-D-ribosyl)-ATP + H2O = 1-(5-phospho-β-D-ribosyl)-5'-AMP + diphosphate + H+UniRule annotationEC:3.6.1.31UniRule annotation
: L-histidine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotationProteins known to be involved in the 9 steps of the subpathway in this organism are:
- ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
- Phosphoribosyl-ATP pyrophosphatase (hisE), Phosphoribosyl-ATP pyrophosphatase (hisE)
- Phosphoribosyl-AMP cyclohydrolase (hisI), Phosphoribosyl-AMP cyclohydrolase (hisI)
- 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
- Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
- Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
- Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase (hisC)
- Histidinol-phosphatase (EJ379_07170), Histidinol-phosphatase (BC_1413)
- Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- phosphoribosyl-ATP diphosphatase activity Source: UniProtKB-UniRule
GO - Biological processi
- histidine biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase |
Biological process | Amino-acid biosynthesis, Histidine biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00031;UER00007 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphoribosyl-ATP pyrophosphataseUniRule annotation (EC:3.6.1.31UniRule annotation)Short name: PRA-PHUniRule annotation |
Gene namesi | Name:hisEUniRule annotation Ordered Locus Names:BC_1412 |
Organismi | Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711) |
Taxonomic identifieri | 226900 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000136345 | 1 – 107 | Phosphoribosyl-ATP pyrophosphataseAdd BLAST | 107 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q81G00 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q81G00 |
Family & Domainsi
Sequence similaritiesi
Belongs to the PRA-PH family.UniRule annotation
Phylogenomic databases
HOGENOMi | CLU_123337_0_0_9 |
OMAi | FTHEKGE |
Family and domain databases
CDDi | cd11534, NTP-PPase_HisIE_like, 1 hit |
HAMAPi | MF_01020, HisE, 1 hit |
InterProi | View protein in InterPro IPR008179, HisE IPR021130, PRib-ATP_PPHydrolase-like |
Pfami | View protein in Pfam PF01503, PRA-PH, 1 hit |
TIGRFAMsi | TIGR03188, histidine_hisI, 1 hit |
i Sequence
Sequence statusi: Complete.
Q81G00-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MENAFKLLYK TIEERKGSPL PESYTNYLFS KGEDKILKKI GEECAEVIIA
60 70 80 90 100
CKNNDKEEVV KEMVDVFYHC FVLLAEKNIA LEDVMREVKE RNGKLSRVGD
RREIDTL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE016877 Genomic DNA Translation: AAP08393.1 |
RefSeqi | NP_831192.1, NC_004722.1 WP_000426358.1, NZ_CP034551.1 |
Genome annotation databases
EnsemblBacteriai | AAP08393; AAP08393; BC_1412 |
GeneIDi | 50192193 |
KEGGi | bce:BC1412 |
PATRICi | fig|226900.8.peg.1389 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE016877 Genomic DNA Translation: AAP08393.1 |
RefSeqi | NP_831192.1, NC_004722.1 WP_000426358.1, NZ_CP034551.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1YVW | X-ray | 2.60 | A/B/C/D | 1-107 | [»] | |
SMRi | Q81G00 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
EnsemblBacteriai | AAP08393; AAP08393; BC_1412 |
GeneIDi | 50192193 |
KEGGi | bce:BC1412 |
PATRICi | fig|226900.8.peg.1389 |
Phylogenomic databases
HOGENOMi | CLU_123337_0_0_9 |
OMAi | FTHEKGE |
Enzyme and pathway databases
UniPathwayi | UPA00031;UER00007 |
Miscellaneous databases
EvolutionaryTracei | Q81G00 |
Family and domain databases
CDDi | cd11534, NTP-PPase_HisIE_like, 1 hit |
HAMAPi | MF_01020, HisE, 1 hit |
InterProi | View protein in InterPro IPR008179, HisE IPR021130, PRib-ATP_PPHydrolase-like |
Pfami | View protein in Pfam PF01503, PRA-PH, 1 hit |
TIGRFAMsi | TIGR03188, histidine_hisI, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HIS2_BACCR | |
Accessioni | Q81G00Primary (citable) accession number: Q81G00 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 15, 2004 |
Last sequence update: | June 1, 2003 | |
Last modified: | December 2, 2020 | |
This is version 108 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families