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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Status
Reviewed-Annotation score: -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: 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).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 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.

Pathwayi: 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.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 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

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

BioCyciPPEN278197:G1G70-1429-MONOMER
UniPathwayi
UPA00074;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:PEPE_1458
OrganismiPediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Taxonomic identifieri278197 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaePediococcus
Proteomesi
  • UP000000773 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000189221 – 511Bifunctional purine biosynthesis protein PurHAdd BLAST511

Proteomic databases

PRIDEiQ03E83

Interactioni

Protein-protein interaction databases

STRINGi278197.PEPE_1458

Structurei

3D structure databases

ProteinModelPortaliQ03E83
SMRiQ03E83
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 144MGS-likePROSITE-ProRule annotationAdd BLAST144

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DC1 Bacteria
COG0138 LUCA
HOGENOMiHOG000230373
KOiK00602
OMAiDLLFAWK
OrthoDBiPOG091H00UT

Family and domain databases

Gene3Di3.40.140.20, 2 hits
3.40.50.1380, 1 hit
HAMAPiMF_00139 PurH, 1 hit
InterProiView protein in InterPro
IPR024051 AICAR_Tfase_dup_dom_sf
IPR016193 Cytidine_deaminase-like
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR002695 PurH-like
PANTHERiPTHR11692 PTHR11692, 1 hit
PfamiView protein in Pfam
PF01808 AICARFT_IMPCHas, 1 hit
PF02142 MGS, 1 hit
PIRSFiPIRSF000414 AICARFT_IMPCHas, 1 hit
SMARTiView protein in SMART
SM00798 AICARFT_IMPCHas, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF52335 SSF52335, 1 hit
SSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR00355 purH, 1 hit
PROSITEiView protein in PROSITE
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q03E83-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTALLSVSD KTGIVEFARG LVKADFRIIS TGGTKKVLEE AGLSIVSVEA
60 70 80 90 100
ITNFPEMLDG RVKTLHPAIH GGLLARRDLP EHLAALKEHN IDLIDLVCVN
110 120 130 140 150
LYPFKSTIMQ NGVTEAEAIE QIDIGGPSML RSAAKNFASV LPVVDPKDYQ
160 170 180 190 200
PVLAALAHQT DNVKFRRALA LKVFQHTAAY DTLIAQYLGQ NGEIFPDELT
210 220 230 240 250
KTYTKKQVMR YGENSHQKAA FYEDALPVPF SIAQAQQLHG KELSYNNIKD
260 270 280 290 300
ADAALKMSAE FNQPAVVAVK HMNPCGIGLG QNIEEAWDRA YEADSMSIFG
310 320 330 340 350
GIIVLNRPVD LATAEKMHKL FLEIIIAPSF EKEAFTVLAQ KKNLRIMTVD
360 370 380 390 400
FNQHQDAKEL ETVSVMGGLL VQEQDAVVET ATDFKVVSKR QPTESELKAM
410 420 430 440 450
VFGQTVVKHV KSNAIVITTD QQTLGIGAGQ MNRIGSVEIA VKQAEGSANF
460 470 480 490 500
KNAVMASDAF FPMEDCVEYA AKHGIKAIVE PGGSIKDQAS IDKADELGIS
510
LIFSGRRHFR H
Length:511
Mass (Da):55,930
Last modified:November 14, 2006 - v1
Checksum:iB4020CBDB5383A91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000422 Genomic DNA Translation: ABJ68489.1
RefSeqiWP_011673675.1, NC_008525.1

Genome annotation databases

EnsemblBacteriaiABJ68489; ABJ68489; PEPE_1458
GeneIDi33062466
KEGGippe:PEPE_1458

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000422 Genomic DNA Translation: ABJ68489.1
RefSeqiWP_011673675.1, NC_008525.1

3D structure databases

ProteinModelPortaliQ03E83
SMRiQ03E83
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi278197.PEPE_1458

Proteomic databases

PRIDEiQ03E83

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ68489; ABJ68489; PEPE_1458
GeneIDi33062466
KEGGippe:PEPE_1458

Phylogenomic databases

eggNOGiENOG4105DC1 Bacteria
COG0138 LUCA
HOGENOMiHOG000230373
KOiK00602
OMAiDLLFAWK
OrthoDBiPOG091H00UT

Enzyme and pathway databases

UniPathwayi
UPA00074;UER00133

UPA00074;UER00135

BioCyciPPEN278197:G1G70-1429-MONOMER

Family and domain databases

Gene3Di3.40.140.20, 2 hits
3.40.50.1380, 1 hit
HAMAPiMF_00139 PurH, 1 hit
InterProiView protein in InterPro
IPR024051 AICAR_Tfase_dup_dom_sf
IPR016193 Cytidine_deaminase-like
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR002695 PurH-like
PANTHERiPTHR11692 PTHR11692, 1 hit
PfamiView protein in Pfam
PF01808 AICARFT_IMPCHas, 1 hit
PF02142 MGS, 1 hit
PIRSFiPIRSF000414 AICARFT_IMPCHas, 1 hit
SMARTiView protein in SMART
SM00798 AICARFT_IMPCHas, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF52335 SSF52335, 1 hit
SSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR00355 purH, 1 hit
PROSITEiView protein in PROSITE
PS51855 MGS, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPUR9_PEDPA
AccessioniPrimary (citable) accession number: Q03E83
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: October 10, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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