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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route).
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH), Bifunctional purine biosynthesis protein PurH (purH)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH), Bifunctional purine biosynthesis protein PurH (purH)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
  • biofilm formation Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:AICARTRANSIMPCYCLO-CPLX.
ECOL316407:JW3970-MONOMER.
MetaCyc:AICARTRANSIMPCYCLO-CPLX.
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:b4006, JW3970
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10795. purH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Bifunctional purine biosynthesis protein PurHPRO_0000192091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP15639.
PRIDEiP15639.

2D gel databases

SWISS-2DPAGEP15639.

Interactioni

Protein-protein interaction databases

IntActiP15639. 7 interactions.
STRINGi511145.b4006.

Structurei

3D structure databases

ProteinModelPortaliP15639.
SMRiP15639. Positions 4-529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiP15639.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.
PhylomeDBiP15639.

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.

P15639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM
110 120 130 140 150
VVVNLYPFAQ TVAREGCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS
160 170 180 190 200
SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF EHTAAYDSMI ANYFGSMVPA
210 220 230 240 250
YHGESKEAAG RFPRTLNLNF IKKLDMRYGE NSHQQAAFYI EENVKEASVA
260 270 280 290 300
TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI
310 320 330 340 350
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE
360 370 380 390 400
EALKITAAKQ NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE
410 420 430 440 450
LRVVTKRQPS EQELRDALFC WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR
460 470 480 490 500
VYSAKIAGIK AADEGLEVKG SSMASDAFFP FRDGIDAAAA AGVTCVIQPG
510 520
GSIRDDEVIA AADEHGIAML FTDMRHFRH
Length:529
Mass (Da):57,329
Last modified:April 1, 1990 - v1
Checksum:iDC034ED01915DA68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05126 Genomic DNA. Translation: AAA24454.1.
X51950 Genomic DNA. Translation: CAA36212.1.
U00006 Genomic DNA. Translation: AAC43104.1.
U00096 Genomic DNA. Translation: AAC76980.1.
AP009048 Genomic DNA. Translation: BAE77313.1.
PIRiB34193. DTECPH.
RefSeqiNP_418434.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76980; AAC76980; b4006.
BAE77313; BAE77313; BAE77313.
GeneIDi948503.
KEGGiecj:Y75_p3190.
eco:b4006.
PATRICi32123537. VBIEscCol129921_4121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05126 Genomic DNA. Translation: AAA24454.1.
X51950 Genomic DNA. Translation: CAA36212.1.
U00006 Genomic DNA. Translation: AAC43104.1.
U00096 Genomic DNA. Translation: AAC76980.1.
AP009048 Genomic DNA. Translation: BAE77313.1.
PIRiB34193. DTECPH.
RefSeqiNP_418434.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP15639.
SMRiP15639. Positions 4-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15639. 7 interactions.
STRINGi511145.b4006.

2D gel databases

SWISS-2DPAGEP15639.

Proteomic databases

PaxDbiP15639.
PRIDEiP15639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76980; AAC76980; b4006.
BAE77313; BAE77313; BAE77313.
GeneIDi948503.
KEGGiecj:Y75_p3190.
eco:b4006.
PATRICi32123537. VBIEscCol129921_4121.

Organism-specific databases

EchoBASEiEB0788.
EcoGeneiEG10795. purH.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiP15639.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.
PhylomeDBiP15639.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciEcoCyc:AICARTRANSIMPCYCLO-CPLX.
ECOL316407:JW3970-MONOMER.
MetaCyc:AICARTRANSIMPCYCLO-CPLX.

Miscellaneous databases

PROiP15639.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli."
    Aiba A., Mizobuchi K.
    J. Biol. Chem. 264:21239-21246(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus."
    Flannigan K.A., Hennigan S.H., Vogelbacker H.H., Gots J.S., Smith J.M.
    Mol. Microbiol. 4:381-392(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiPUR9_ECOLI
AccessioniPrimary (citable) accession number: P15639
Secondary accession number(s): Q2M8U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 24, 2015
This is version 129 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, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.