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P15639

- PUR9_ECOLI

UniProt

P15639 - PUR9_ECOLI

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Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, b4006, JW3970
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 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.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: EcoCyc
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: EcoCyc

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10795. purH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_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.

Expressioni

Gene expression databases

GenevestigatoriP15639.

Interactioni

Protein-protein interaction databases

IntActiP15639. 7 interactions.
STRINGi511145.b4006.

Structurei

3D structure databases

ProteinModelPortaliP15639.
SMRiP15639. Positions 4-529.

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.
HOGENOMiHOG000230372.
KOiK00602.
OMAiRAFKTDP.
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

MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP    50
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM 100
VVVNLYPFAQ TVAREGCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS 150
SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF EHTAAYDSMI ANYFGSMVPA 200
YHGESKEAAG RFPRTLNLNF IKKLDMRYGE NSHQQAAFYI EENVKEASVA 250
TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI 300
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE 350
EALKITAAKQ NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE 400
LRVVTKRQPS EQELRDALFC WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR 450
VYSAKIAGIK AADEGLEVKG SSMASDAFFP FRDGIDAAAA AGVTCVIQPG 500
GSIRDDEVIA AADEHGIAML FTDMRHFRH 529
Length:529
Mass (Da):57,329
Last modified:April 1, 1990 - v1
Checksum:iDC034ED01915DA68
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_491454.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76980; AAC76980; b4006.
BAE77313; BAE77313; BAE77313.
GeneIDi12933467.
948503.
KEGGiecj:Y75_p3190.
eco:b4006.
PATRICi32123537. VBIEscCol129921_4121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi B34193. DTECPH.
RefSeqi NP_418434.1. NC_000913.3.
YP_491454.1. NC_007779.1.

3D structure databases

ProteinModelPortali P15639.
SMRi P15639. Positions 4-529.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P15639. 7 interactions.
STRINGi 511145.b4006.

2D gel databases

SWISS-2DPAGE P15639.

Proteomic databases

PaxDbi P15639.
PRIDEi P15639.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76980 ; AAC76980 ; b4006 .
BAE77313 ; BAE77313 ; BAE77313 .
GeneIDi 12933467.
948503.
KEGGi ecj:Y75_p3190.
eco:b4006.
PATRICi 32123537. VBIEscCol129921_4121.

Organism-specific databases

EchoBASEi EB0788.
EcoGenei EG10795. purH.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230372.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.
PhylomeDBi P15639.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci EcoCyc:AICARTRANSIMPCYCLO-CPLX.
ECOL316407:JW3970-MONOMER.
MetaCyc:AICARTRANSIMPCYCLO-CPLX.

Miscellaneous databases

PROi P15639.

Gene expression databases

Genevestigatori P15639.

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

« 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: May 14, 2014
This is version 123 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

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