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Q9ZHE7 (HIS1_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP phosphoribosyltransferase

Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17
Gene names
Name:hisG
Ordered Locus Names:BUsg_092
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity By similarity. HAMAP-Rule MF_00079

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00079

Enzyme regulation

Feedback inhibited by histidine By similarity. HAMAP-Rule MF_00079

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP-Rule MF_00079

Subunit structure

Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00079.

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_0000151834

Experimental info

Sequence conflict143 – 1453NIV → TL Ref.1
Sequence conflict147 – 1482KS → QV Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ZHE7 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 8E0858F490DFF1C0

FASTA29933,349
        10         20         30         40         50         60 
MFNTNRVRIA MQKTGRLSSE SIKLLTCCGI KINLKQQKLI AFAENMPIDV MLVRDDDIPG 

        70         80         90        100        110        120 
LVMDGVVDLG IVGENVLQEE LLHRISQNLE NSYITLRRLD FGICRLSLAI PINTPYVDIT 

       130        140        150        160        170        180 
SLKNFRIATS YPHLLKKYLD SKNIVFKSCM LNGSVEVAPR AGLADAICDL VSTGATLEAN 

       190        200        210        220        230        240 
GLREVQVVFR SHACLICKTG NINFAKKEVI NKLMTRIKGV IKARESKYIM LHAPVNKLEE 

       250        260        270        280        290 
VISLLHGAEK PTILKLAGDD HRVAMHMVSS ETLFWETMEK LKSLGASSIL VLPIEKMME 

« Hide

References

« Hide 'large scale' references
[1]"Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis."
Clark M.A., Baumann L., Baumann P.
Curr. Microbiol. 37:356-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067228 Genomic DNA. Translation: AAC97354.1.
AE013218 Genomic DNA. Translation: AAM67662.1.
RefSeqNP_660451.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ9ZHE7.
SMRQ9ZHE7. Positions 6-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg092.

Proteomic databases

PRIDEQ9ZHE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67662; AAM67662; BUsg_092.
GeneID1005909.
KEGGbas:BUsg092.
PATRIC21246961. VBIBucAph100086_0095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
KOK00765.
OMAVATEFPN.
OrthoDBEOG66MQT3.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-101-MONOMER.
UniPathwayUPA00031; UER00006.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
HAMAPMF_00079. HisG_Long.
InterProIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]
PANTHERPTHR21403. PTHR21403. 1 hit.
PfamPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
SUPFAMSSF54913. SSF54913. 1 hit.
TIGRFAMsTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS1_BUCAP
AccessionPrimary (citable) accession number: Q9ZHE7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 30, 2002
Last modified: February 19, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names