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B0RSL3 (HIS1_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:xcc-b100_2095
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length304 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: 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 – 304304ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_1000092759

Sequences

Sequence LengthMass (Da)Tools
B0RSL3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: B4D065E68B630AF3

FASTA30432,748
        10         20         30         40         50         60 
MSASTAAPAR DRLRIAIQKN GRLAEPARSL LAACGLSWRQ SRDKLFCYGE SLPVDLLLVR 

        70         80         90        100        110        120 
DDDIPGLIAD GVCDLGIVGQ NELDEQASAR RRAGLPAAYH AVRGVGFGQC RLMLAVPEEW 

       130        140        150        160        170        180 
EWQGVAQLAG KRIATSYPAI LADWLERQGI DASVVELSGS VEIAPRLGTA DLICDLVSSG 

       190        200        210        220        230        240 
ATLAANQLKP VELVMESEAV LAGAVREPAD ARAALLAMLL RRMDGVLKLR DSKLLMFRAE 

       250        260        270        280        290        300 
QGNVDALRRL LPDADPLVQL PDDGNGALRL QTMCHGAVTW QRLEELERAG AQGLMVLTVE 


RSLA 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP51448.1.
RefSeqYP_001903500.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RSL3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_2095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP51448; CAP51448; xcc-b100_2095.
GeneID6322205.
KEGGxca:xccb100_2095.
PATRIC24084085. VBIXanCam108527_2131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
KOK00765.
OMAYSKASMR.
OrthoDBEOG66MQT3.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-2140-MONOMER.
UniPathwayUPA00031; UER00006.

Family and domain databases

HAMAPMF_00079. HisG_Long.
InterProIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
[Graphical view]
PANTHERPTHR21403. PTHR21403. 1 hit.
PfamPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS1_XANCB
AccessionPrimary (citable) accession number: B0RSL3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 47 of the entry and version 1 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