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Q6HLE1 (HIS2_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoribosyl-ATP pyrophosphatase

Short name=PRA-PH
EC=3.6.1.31
Gene names
Name:hisE
Ordered Locus Names:BT9727_1296
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01020

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01020

Subcellular location

Cytoplasm By similarity HAMAP MF_01020.

Sequence similarities

Belongs to the PRA-PH family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosyl-ATP diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 107107Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020
PRO_0000230167

Sequences

Sequence LengthMass (Da)Tools
Q6HLE1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 38F03898C7351E2D

FASTA10712,466
        10         20         30         40         50         60 
MRNAFTLLFE TIEERKNNPL PESYTNYLFS KGEDKILKKI GEECSEVIIA SKNNDNEELV 

        70         80         90        100 
KEMVDVLYHC FVLLAEKNIP LKDIMEEVTE RNGKLSRVGD RREIDTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT59424.1.
RefSeqYP_035630.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HLE1.
SMRQ6HLE1. Positions 4-95.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000073294; EBBACP00000071380; EBBACG00000073285.
GeneID2856158.
GenomeReviewsGene locus BT9727_1296 in contig AE017355_GR.
KEGGbtk:BT9727_1296.
NMPDRfig|281309.1.peg.1270.
PATRIC18983271. VBIBacThu119411_1365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000893.
HOGENOMHBG646527.
OMACSEVIIA.
ProtClustDBPRK00400.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_1296-MONOMER.

Family and domain databases

HAMAPMF_01020. HisE.
[Tree]
InterProIPR023287. alpha_NTP_pyrophos_dom.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
[Graphical view]
Gene3DG3DSA:1.10.3310.10. G3DSA:1.10.3310.10. 1 hit.
KOK01523.
PfamPF01503. PRA-PH. 1 hit.
[Graphical view]
TIGRFAMsTIGR03188. Histidine_hisI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS2_BACHK
AccessionPrimary (citable) accession number: Q6HLE1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families