SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q87D58

- PUR9_XYLFT

UniProt

Q87D58 - PUR9_XYLFT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH, PD_0828
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciXFAS183190:GIX4-828-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:PD_0828
OrganismiXylella fastidiosa (strain Temecula1 / ATCC 700964)
Taxonomic identifieri183190 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
ProteomesiUP000002516: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_0000192152Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi183190.PD0828.

Structurei

3D structure databases

ProteinModelPortaliQ87D58.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
KOiK00602.
OMAiRAFKTDP.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q87D58-1 [UniParc]FASTAAdd to Basket

« Hide

MASDFLPVHR ALLSVSDKTG LVELARVLLA YNIELLSTGG TATIIREAGL    50
PVQDVADLTD FPEMMDGRVK TLHPVVHGGL LGRAGIDDAV MAKHGIAPID 100
LLIVNLYPFE QITAKKDCTL ADAVDTIDIG GPAMLRSAAK NFARVAVATS 150
PDQYPDLLAE LQAHHGQLSA EKRFALAVAA FNHVAQYDAA ISNYLSSVSD 200
MHTTLPLRHE FPTQLNNTFV KMTDLRYGEN PHQSGAFYRD VHPQPGTLAT 250
FKQLQGKRLS YNNLVDADAA WECVRQFEAP ACVIVKHANP CGVAVGTACS 300
DAYEAAYATD PTSAFGGIIA FNRTLDAVTM QSILDRQFVE VLIAPYYDAD 350
ALAYATKKAN VRVLRIPSTG AMNRYDFKRI GSGLLVQSAD SLNIHSGALK 400
VVTQLAPTYA QQRDLLFAWH VAKYVKSNAI VYAKDNRTIG IGAGQMSRVY 450
SARIAGIKAA DAHLAVTGSV MASDAFFPFR DGIDAAAATG IKAVIQPGGS 500
MRDNEVIAAA DEHGIAMVFT GIRHFRH 527
Length:527
Mass (Da):56,725
Last modified:June 16, 2003 - v1
Checksum:i3265D4F5E6BED741
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28696.1.
RefSeqiNP_779047.1. NC_004556.1.

Genome annotation databases

EnsemblBacteriaiAAO28696; AAO28696; PD_0828.
GeneIDi1143550.
KEGGixft:PD0828.
PATRICi24149535. VBIXylFas71109_1081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28696.1 .
RefSeqi NP_779047.1. NC_004556.1.

3D structure databases

ProteinModelPortali Q87D58.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 183190.PD0828.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO28696 ; AAO28696 ; PD_0828 .
GeneIDi 1143550.
KEGGi xft:PD0828.
PATRICi 24149535. VBIXylFas71109_1081.

Phylogenomic databases

eggNOGi COG0138.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci XFAS183190:GIX4-828-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa."
    Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.
    , Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.
    J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Temecula1 / ATCC 700964.

Entry informationi

Entry nameiPUR9_XYLFT
AccessioniPrimary (citable) accession number: Q87D58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi