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Q8DIN5

- PUR9_THEEB

UniProt

Q8DIN5 - PUR9_THEEB

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Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, tlr1547
Organism
Thermosynechococcus elongatus (strain BP-1)
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

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:tlr1547
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_0000192140Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi197221.tlr1547.

Structurei

3D structure databases

ProteinModelPortaliQ8DIN5.

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.
HOGENOMiHOG000230373.
KOiK00602.
OMAiCGVATGP.
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.

Q8DIN5-1 [UniParc]FASTAAdd to Basket

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MGRMALLSTS NKQGLVELAR ALVQEFGFTL LSSGGTAKAL QTAGIPVTTV    50
SEYTGAPEIL GGRVKTLHPK IHGGILARRD RPQDEADLQA QAIHPIDLVV 100
VNLYPFAETI AQPNVTLAEA IEQIDIGGPT LIRAAAKNHA HVTVLVDPSQ 150
YETYLQELRL YGDAQPAFRL ACAQQAFALT AHYDQAIAEY LQKVTAAGTE 200
PEILPPVFHL TGRQKQVLRY GENPHQRASW YVCGAHPRGW AAAHLLQGKE 250
LSYNNLLDLE AARGVISEFL GDSPPAAVII KHTNPCGVAE GKTLVEAYER 300
AFAADRVSAF GGIVALNRPL DGATAEALTR TFLECVVAPA CEEAALPILK 350
TKPKMRVLTL PELHRAPTTA IQTIAGGFLV QEIHPLPIDP EAWQVVTATE 400
PSPELMAELI FAWKVVKHVK SNAIVVSRDR QTQGIGAGQM NRVGAVEIAL 450
SAAGEAARGG VLASDGFFPF ADSVEAAALA GIAAIIQPGG SLRDSESIQA 500
ANAAGIAMVF TNQRHFRH 518
Length:518
Mass (Da):55,271
Last modified:March 1, 2003 - v1
Checksum:iF1010485BADCEFB6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC09099.1.
RefSeqiNP_682337.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09099; BAC09099; BAC09099.
GeneIDi1011044.
KEGGitel:tlr1547.
PATRICi23928458. VBITheElo119873_1623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC09099.1 .
RefSeqi NP_682337.1. NC_004113.1.

3D structure databases

ProteinModelPortali Q8DIN5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 197221.tlr1547.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC09099 ; BAC09099 ; BAC09099 .
GeneIDi 1011044.
KEGGi tel:tlr1547.
PATRICi 23928458. VBITheElo119873_1623.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi CGVATGP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiPUR9_THEEB
AccessioniPrimary (citable) accession number: Q8DIN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 69 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

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