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A3MSF5 (HIS1_PYRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 48. 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:
ATP phosphoribosyltransferase

Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17
Gene names
Name:hisG
Ordered Locus Names:Pcal_0134
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length282 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

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: 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 – 282282ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_1000004488

Sequences

Sequence LengthMass (Da)Tools
A3MSF5 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 2298655D87E54292

FASTA28230,495
        10         20         30         40         50         60 
MLLAIPSKGR LLDPTLKLLE AIGMRLLASD ERALVVPTSW RDVNVIRARP EDIPYIVESG 

        70         80         90        100        110        120 
KVWAGVTGHD YVVESGASVV EALELGFGRG RLVVAVPKSS GIKTVDELPP GTRVATKFVN 

       130        140        150        160        170        180 
IAYNYFAELG KRVRVVRVTG SVEILPQLGI ADAILDVMAT GTTLEVHGLV PIATVLETSA 

       190        200        210        220        230        240 
RLIVHPSYVN HELTKKLTTF IQGYYAAQGK KMIFLNVPAS RLEKVLAVLP AMEAPSVTPL 

       250        260        270        280 
AKGDVYEVFS VVPEDELPDI VIRLKEAGAK DIVVTPIEKL IS 

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000561 Genomic DNA. Translation: ABO07572.1.
RefSeqYP_001055038.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MSF5.
ModBaseSearch...

Protein-protein interaction databases

STRING410359.Pcal_0134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO07572; ABO07572; Pcal_0134.
GeneID4908524.
KEGGpcl:Pcal_0134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223247.
KOK00765.
OMAVATEFPN.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycPCAL410359:GIX2-136-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. N-reg_PII-like_a/b. 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_PYRCJ
AccessionPrimary (citable) accession number: A3MSF5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 29, 2013
This is version 48 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