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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Status
Reviewed-Annotation score: Annotation score: 2 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-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciDSHI398580:GKEL-360-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:Dshi_0358
OrganismiDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Taxonomic identifieri398580 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter
ProteomesiUP000006833 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Bifunctional purine biosynthesis protein PurHPRO_1000076480Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi398580.Dshi_0358.

Structurei

3D structure databases

ProteinModelPortaliA8LMD0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
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.

A8LMD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDLVPLRRA LLSVSDKTGL VPLGQALAAR GVELLSTGGT AKALREAGLD
60 70 80 90 100
VVDVSDVTGF PEMMDGRVKT LHPKVHGGLL ALRDNAAHVS AMERHGIGAI
110 120 130 140 150
DLLVVNLYPF EATVAAGADY AACIENIDIG GPAMIRAAAK NHSFVTVLTD
160 170 180 190 200
VEDYEALLGE LEAREGATGY PFRQKMALNA YARTAAYDAA VSGWMTDALA
210 220 230 240 250
EVAPRRRAVA GTLAQTLRYG ENPHQGAAFY VDGSDRPGVA TAVQHQGKEL
260 270 280 290 300
SYNNINDTDA AFELVAEFAP EDGPACAIIK HANPCGVARG ATLAEAYTKA
310 320 330 340 350
FQCDQTSAFG GIIALNRPLD GPTAEAISGI FTEVVIAPGA DETARAVFAA
360 370 380 390 400
KKNLRLLTTE GLPDPKAPAL TVRQVSGGYL VQDKDNGNIG WDDLKVVTKR
410 420 430 440 450
APSEAEIADL LFAWKVAKHV KSNAIVYVKD GATVGVGAGQ MSRVDSARIA
460 470 480 490 500
ARKSADMAEA LGLETPLIQG SVVASDAFFP FPDGLLTAAE AGATAVIQPG
510 520
GSMRDVEVIA AADAAGLAMV FTGMRHFRH
Length:529
Mass (Da):55,301
Last modified:December 3, 2007 - v1
Checksum:i9D80F746B4C28997
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000830 Genomic DNA. Translation: ABV92107.1.
RefSeqiYP_001531708.1. NC_009952.1.

Genome annotation databases

EnsemblBacteriaiABV92107; ABV92107; Dshi_0358.
GeneIDi5711267.
KEGGidsh:Dshi_0358.
PATRICi21813179. VBIDinShi9476_0362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000830 Genomic DNA. Translation: ABV92107.1.
RefSeqiYP_001531708.1. NC_009952.1.

3D structure databases

ProteinModelPortaliA8LMD0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi398580.Dshi_0358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV92107; ABV92107; Dshi_0358.
GeneIDi5711267.
KEGGidsh:Dshi_0358.
PATRICi21813179. VBIDinShi9476_0362.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciDSHI398580:GKEL-360-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 16493 / NCIMB 14021 / DFL 12.

Entry informationi

Entry nameiPUR9_DINSH
AccessioniPrimary (citable) accession number: A8LMD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 19, 2008
Last sequence update: December 3, 2007
Last modified: March 3, 2015
This is version 51 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, Reference proteome

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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.