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A0RBM4 (HIS2_BACAH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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:BALH_1267
OrganismBacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]
Taxonomic identifier412694 [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.

Sequence caution

The sequence ABK84617.1 differs from that shown. Reason: Erroneous initiation.

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_0000319640

Sequences

Sequence LengthMass (Da)Tools
A0RBM4 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: A40DDFC5539EE54A

FASTA10712,427
        10         20         30         40         50         60 
MENTFKLLFE TIGERKRNPL PESYTNYLFS KGEDKILKKI GEECTEVIIA SKNNDKEELV 

        70         80         90        100 
KEMVDVLYHC FVLLAEKNIS LEDIMAEVTE RNGKLSRVGD RREIDTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000485 Genomic DNA. Translation: ABK84617.1. Different initiation.
RefSeqYP_894124.1. NC_008600.1.

3D structure databases

ProteinModelPortalA0RBM4.
SMRA0RBM4. Positions 5-95.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0RBM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000067986; EBBACP00000066223; EBBACG00000067977.
GeneID4546880.
GenomeReviewsGene locus BALH_1267 in contig CP000485_GR.
KEGGbtl:BALH_1267.
PATRIC18994932. VBIBacThu63319_1469.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0140.
GeneTreeEBGT00050000000893.
HOGENOMHBG646527.
ProtClustDBPRK00400.

Enzyme and pathway databases

BioCycBTHU412694:BALH_1267-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_BACAH
AccessionPrimary (citable) accession number: A0RBM4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: December 14, 2011
This is version 40 of the entry and version 2 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