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Q87QL2 (HIS1_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:VP1137
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length298 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.

Sequence caution

The sequence BAC59400.1 differs from that shown. Reason: Erroneous initiation.

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 – 298298ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_0000151870

Sequences

Sequence LengthMass (Da)Tools
Q87QL2 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 1DC3A1620CA4F108

FASTA29832,845
        10         20         30         40         50         60 
MQTQRLRIAI QKKGRLSKES QALLKQCGVK FNVMGERLVV HSENMPIDLL LVRDDDIPGL 

        70         80         90        100        110        120 
IMDGVVDLGF IGENELEEVR LDRKALGEPC EFVQLRRLDF GGCRLSIAID KDEEYNGPQD 

       130        140        150        160        170        180 
LAGKRIATTY PQLLKAYMDE AGVPFSTCML TGSVEVAPRA GLADAIADLV STGATLEANG 

       190        200        210        220        230        240 
LKEAEVIFRS KATLIQRIGE FDADKAELIN KLLTRMQGVQ QAKESKYIML HAPAGKLEQI 

       250        260        270        280        290 
KALLPGAEDP TVLPLSADKQ KVAVHLVSTE NLFWETMEQL KELGASSILV LPIEKMME 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC59400.1. Different initiation.
RefSeqNP_797516.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87QL2.
SMRQ87QL2. Positions 5-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP1137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC59400; BAC59400; BAC59400.
GeneID1188642.
KEGGvpa:VP1137.
PATRIC20140484. VBIVibPar50997_1079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223247.
KOK00765.
OMAVATEFPN.
OrthoDBEOG66MQT3.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-1186-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_VIBPA
AccessionPrimary (citable) accession number: Q87QL2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: February 19, 2014
This is version 74 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