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P77935 (PUR1_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. 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:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPATase
Gene names
Name:purF
Ordered Locus Names:RHE_CH01428
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2121 By similarity
PRO_0000029261
Chain22 – 496475Amidophosphoribosyltransferase
PRO_0000029262

Regions

Domain22 – 241220Glutamine amidotransferase type-2

Sites

Active site221Nucleophile By similarity
Metal binding3711Magnesium By similarity
Metal binding3721Magnesium By similarity

Experimental info

Sequence conflict193 – 1942RD → SH in AAB06461. Ref.1
Sequence conflict3121P → S in AAB06461. Ref.1
Sequence conflict3151L → G in AAB06461. Ref.1
Sequence conflict3271Y → YEY in AAB06461. Ref.1
Sequence conflict4071P → R in AAB06461. Ref.1
Sequence conflict412 – 4176IDTPDA → SIRPTP in AAB06461. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P77935 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: EA8F1F6F9189915C

FASTA49654,162
        10         20         30         40         50         60 
MNQSHSFPTD DPLDGDTLHE ECGVFGILGH PDAAALTALG LHALQHRGQE AAGIVSFDGK 

        70         80         90        100        110        120 
RFYQERHMGL VGDHYTNPMT LARLPGSISI GHTRYSTTGE VAMRNVQPLF AELEEGGIAI 

       130        140        150        160        170        180 
AHNGNFTNGL TLRRQIIATG AICQSTSDTE VVLHLIARSR HASTSDRFID AIRQMEGGYS 

       190        200        210        220        230        240 
MLAMTRTKLI AARDPTGIRP LVMGELDGKP IFCSETCALD IIGAKFIRDV ENGEVIICEI 

       250        260        270        280        290        300 
QPDGSISIDA RKPSKPQPER LCLFEYVYFA RPDSVVGGRN VYTTRKNMGM NLAKESPVDA 

       310        320        330        340        350        360 
DVVVPVPDGG TPAALGYAQE SGIPFEYGII RNHYVGRTFI EPTQQIRAFG VKLKHSANRA 

       370        380        390        400        410        420 
MIEGKRVVLV DDSIVRGTTS LKIVQMIREA GAREVHIRVA SPMIFFPDFY GIDTPDADKL 

       430        440        450        460        470        480 
LANQYADVEA MAKYIGADSL AFLSINGLYR AVGGEDRNPA RPQFTDHYFT GDYPTRLLDK 

       490 
NGESMGNKLS MLASNG 

« Hide

References

« Hide 'large scale' references
[1]Soberon M., Lopez O., Girard L., Miranda J., Morera C.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CE3.
[2]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65392 Genomic DNA. Translation: AAB06461.1.
CP000133 Genomic DNA. Translation: ABC90231.1.
RefSeqYP_468958.1. NC_007761.1.

3D structure databases

ProteinModelPortalP77935.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347834.RHE_CH01428.

Protein family/group databases

MEROPSC44.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC90231; ABC90231; RHE_CH01428.
GeneID3892667.
KEGGret:RHE_CH01428.
PATRIC23084261. VBIRhiEtl108884_1802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033688.
KOK00764.
OMACDACFTG.
OrthoDBEOG6KT2Q1.
ProtClustDBPRK09123.

Enzyme and pathway databases

BioCycRETL347834:GJJ0-1437-MONOMER.
UniPathwayUPA00074; UER00124.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF13537. GATase_7. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR1_RHIEC
AccessionPrimary (citable) accession number: P77935
Secondary accession number(s): Q2KAA5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 21, 2011
Last modified: November 13, 2013
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