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Q8D8P9 (HIS1_VIBVU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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:VV1_2920
OrganismVibrio vulnificus (strain CMCP6) [Complete proteome] [HAMAP]
Taxonomic identifier216895 [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.

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-HAMAP

   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-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_0000151871

Sequences

Sequence LengthMass (Da)Tools
Q8D8P9 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 3B3B975B9CE8B5E7

FASTA29832,911
        10         20         30         40         50         60 
MQTQRLRIAI QKKGRLSEEC QGLLKKCGVK FNIMGERLVV HSENMPIDLL LVRDDDIPGL 

        70         80         90        100        110        120 
IMDGVVDLGF IGENVLEEVR LERKATGDAC QFETLSRLDF GGCRLSIAID KDEKYNGPQD 

       130        140        150        160        170        180 
LAGKRIATTY PQLLKAYMDR QGVPFSTCML TGSVEVAPRA GLADAIADLV STGATLEANG 

       190        200        210        220        230        240 
LKEAEVIFQS KATLIQRSGE FAQDKQALIE KLLTRMQGVQ QAKESKYIML HAPVDKLEQI 

       250        260        270        280        290 
KALLPGAEDP TVLPLSAEKQ RVAVHLVSTE NLFWETMEQL KELGASSILV LPIEKMME 

« Hide

References

[1]"Complete genome sequence of Vibrio vulnificus CMCP6."
Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CMCP6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016795 Genomic DNA. Translation: AAO11253.2.
RefSeqNP_761726.2. NC_004459.3.

3D structure databases

ProteinModelPortalQ8D8P9.
SMRQ8D8P9. Positions 5-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216895.VV1_2920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO11253; AAO11253; VV1_2920.
GeneID1179756.
KEGGvvu:VV1_2920.
PATRIC20162817. VBIVibVul94426_2883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223247.
KOK00765.
OMATRMQGVI.
OrthoDBEOG66MQT3.

Enzyme and pathway databases

BioCycVVUL216895:GIYM-2640-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_VIBVU
AccessionPrimary (citable) accession number: Q8D8P9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: June 11, 2014
This is version 81 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