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B4SCC0 (HIS1_PELPB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 39. 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:Ppha_0371
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length294 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 – 294294ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_1000092740

Sequences

Sequence LengthMass (Da)Tools
B4SCC0 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 7E7B38DC8292C149

FASTA29432,474
        10         20         30         40         50         60 
MDSINQVLKL GLPKGSLQDS TIDLFAQAGF HFSVQSRSYF PSIDDDELEA ILIRAQEMAH 

        70         80         90        100        110        120 
YVELGAFDVG LTGKDWIIET DADVVEVADL VYSKASMRPV RWVLCVPESS TVRSVKDLEG 

       130        140        150        160        170        180 
KHIATEVVNI TRKYLAKNGV NAMVEFSWGA TEVKPPDLAD AIVEVTETGS SLRANKLRIV 

       190        200        210        220        230        240 
DTILESNTKL IANKASWNDP WKREKIENMA MLLLGAINAQ GKVGLKMNAP KSAIDKILAI 

       250        260        270        280        290 
IPALRQPTIS SLAEEQWVAL EVIVSEKTVR KLIPELKRAG AEGIFEYNIN KLID 

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001110 Genomic DNA. Translation: ACF42700.1.
RefSeqYP_002017317.1. NC_011060.1.

3D structure databases

ProteinModelPortalB4SCC0.
ModBaseSearch...

Protein-protein interaction databases

STRING324925.Ppha_0371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF42700; ACF42700; Ppha_0371.
GeneID6462412.
KEGGpph:Ppha_0371.
PATRIC22901160. VBIPelPha134556_0375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223250.
KOK00765.
OMAEGKHIAT.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycPPHA324925:GHBF-384-MONOMER.
UniPathwayUPA00031; UER00006.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
HAMAPMF_00079. HisG_Long.
InterProIPR013820. ATP_PRibTrfase_cat.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS1_PELPB
AccessionPrimary (citable) accession number: B4SCC0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 29, 2013
This is version 39 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