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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Lactobacillus casei (strain BL23)
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

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:LCABL_19660
OrganismiLactobacillus casei (strain BL23)
Taxonomic identifieri543734 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000960681 – 507Bifunctional purine biosynthesis protein PurHAdd BLAST507

Proteomic databases

PRIDEiB3WF93

Structurei

3D structure databases

ProteinModelPortaliB3WF93
SMRiB3WF93
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

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.

B3WF93-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRALLSVSD KTGLVSFAKG LIDRGFELVS TGGTHRELAA AGIAVTSVEE
60 70 80 90 100
VTGFPEMLDG RVKTLHPKIH AGILARRDDP DHMEALANHD IQPVDLVCVN
110 120 130 140 150
LYPFAATIKR PDVTRAEAIE QIDIGGPSAL RAAAKNSDSV WAVVDPADYE
160 170 180 190 200
AVLTGLDQDD AHLRQKLAAK VFAITAAYDA QIVHYLDPEP FPEHFTPTYT
210 220 230 240 250
KRQDLRYGEN SHQQAAFYVE PDPNPTSLAA AKQLHGKELS YNNIKDADAA
260 270 280 290 300
LAMLREFSEP AVVAVKHMNP CGIGLGKTIE GAWDKAYAAD PMSIFGGIIA
310 320 330 340 350
LNRPVDLATA EKMHKLFLEI IIAPAFDDDA YAVLAKKKNV RLLTINTADT
360 370 380 390 400
PAELGTETTA IYGGLLIQTR DNQTETPADM TVVTTVKPTD EQLKALAFAQ
410 420 430 440 450
TVVKHVKSNA IVVAQADQTL GIGAGQMNRI GSVELALTQA QQNDNFAGAV
460 470 480 490 500
MASDAFFPMD DCVDYAAKHD IKAIIQPGGS IRDKDSIEKA NQYGIAMVTT

GVRHFRH
Length:507
Mass (Da):54,772
Last modified:September 2, 2008 - v1
Checksum:i0325731AA91558D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM177140 Genomic DNA Translation: CAQ67044.1
RefSeqiWP_003599043.1, NC_010999.1

Genome annotation databases

EnsemblBacteriaiCAQ67044; CAQ67044; LCABL_19660
KEGGilcb:LCABL_19660

Similar proteinsi

Entry informationi

Entry nameiPUR9_LACCB
AccessioniPrimary (citable) accession number: B3WF93
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: May 23, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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