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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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

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:CE0937
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Bifunctional purine biosynthesis protein PurHPRO_0000192088Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.CE0937.

Structurei

3D structure databases

ProteinModelPortaliQ8FR29.
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

HOGENOMiHOG000230373.
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.

Q8FR29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEDRKAIKR ALISVYDKTG LEDLAQALHR AGVEIVSTGS TAAKIADLGI
60 70 80 90 100
PVTPVEELTG FPECLEGRVK TLHPKVHAGI LADTRKDDHL RQLDELGVTP
110 120 130 140 150
FQLVVVNLYP FAETVASGAD FDDCVEQIDI GGPSMVRAAA KNHPSVAVVT
160 170 180 190 200
SPGQYEDVVS VLNTGGFSRA ERTKLAAEAF RHTATYDVTV ATWISEQLSA
210 220 230 240 250
ADTELEFPGW IGSTSTLARS LRYGENPHQS AALYVSHGAS GLAQATQLHG
260 270 280 290 300
KEMSYNNYTD SDAAWRAAWD HERPCVAIIK HANPCGIAVS DESIAAAHRQ
310 320 330 340 350
AHACDSVSAF GGVIASNREV SVEMAEQVAE IFTEVIIAPS YEEGAVEVLS
360 370 380 390 400
QKKNIRILQA EAPVREGFET REISGGLLVQ ERDLIHAEGD NPANWTLAAG
410 420 430 440 450
EAVSAEVLKD LEFAWTAVRS VKSNAILLAK DGATVGVGMG QVNRVDSARL
460 470 480 490 500
AVDRAGEERA TGSVAASDAF FPFADGFEVL AQAGITAVVQ PGGSIRDDEV
510 520
IEAANKAGVT MYLTGARHFS H
Length:521
Mass (Da):55,454
Last modified:March 1, 2003 - v1
Checksum:i1FC6B7425B53936E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17747.1.
RefSeqiNP_737547.1. NC_004369.1.
WP_006770098.1. NZ_GG700688.1.

Genome annotation databases

EnsemblBacteriaiBAC17747; BAC17747; BAC17747.
GeneIDi1031951.
KEGGicef:CE0937.
PATRICi21488014. VBICorEff9312_0943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17747.1.
RefSeqiNP_737547.1. NC_004369.1.
WP_006770098.1. NZ_GG700688.1.

3D structure databases

ProteinModelPortaliQ8FR29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.CE0937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC17747; BAC17747; BAC17747.
GeneIDi1031951.
KEGGicef:CE0937.
PATRICi21488014. VBICorEff9312_0943.

Phylogenomic databases

HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiPUR9_COREF
AccessioniPrimary (citable) accession number: Q8FR29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: January 7, 2015
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, 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.