Annotation for this protein is in progress - please check future releases for more complete information



DP00578: AmidophosphoribosyltransferaseFASTA viewXML view

General information
DisProt:DP00578
Name:Amidophosphoribosyltransferase
Synonym(s):PUR1_ECOLI
ATase
EC=2.4.2.14
Glutamine phosphoribosylpyrophosphate amidotransferase
GPATase
First appeared in release:Release 4.5 (07/17/2008)
UniProt:P0AG16
UniGene: 
SwissProt: PUR1_ECOLI
TrEMBL:  
NCBI (GI): 84029594
Source organism:Escherichia coli
Sequence length:505
Percent disordered:12%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH - 60
MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR - 120
RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV - 180
AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF - 240
TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI - 300
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD - 360
KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG - 420
REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD - 480
TLRNDDAKAV QRQNEVENLE MHNEG

Region 2: 73-84 Region 1: 326-350 Region 3: 471-492

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:326 - 350
Length:25
Region sequence:

VKNRYVGRTFIMPGQQLRRKSVRRK

Modification type: Native
PDB: 1ECB:A, 1ECC:A, 1ECF:A, 1ECG:A, 1ECJ:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
 
References:
  1. Smith JL. "Glutamine PRPP amidotransferase: snapshots of an enzyme in action." Curr Opin Struct Biol. 1988; 8(6): 686-94. PubMed: 9914248

Comments:
 



Region 2
Type:Disordered
Name: 
Location:73 - 84
Length:12
Region sequence:

VRYPTAGSSSAS

Modification type: Native
PDB: 1ECB:A, 1ECC:A, 1ECF:A, 1ECG:A, 1ECJ:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
 
References:
  1. Smith JL. "Glutamine PRPP amidotransferase: snapshots of an enzyme in action." Curr Opin Struct Biol. 1988; 8(6): 686-94. PubMed: 9914248

Comments:
 



Region 3
Type:Disordered
Name: 
Location:471 - 492
Length:22
Region sequence:

VDQGYLDFLDTLRNDDAKAVQR

Modification type: Native
PDB: 1ECB:A, 1ECC:A, 1ECF:A, 1ECG:A, 1ECJ:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
 
References:
  1. Smith JL. "Glutamine PRPP amidotransferase: snapshots of an enzyme in action." Curr Opin Struct Biol. 1988; 8(6): 686-94. PubMed: 9914248

Comments:
 



References

  1. Zalkin H. "Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes." Adv Enzyme Regul. 1983; 21: 225-37. PubMed: 6443594


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