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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
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

BioCyciBTHE:G13PU-8783-MONOMER
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:BT_3812
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
Proteomesi
  • UP000001414 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001920711 – 507Bifunctional purine biosynthesis protein PurHAdd BLAST507

Proteomic databases

PaxDbiQ8A155
PRIDEiQ8A155

Interactioni

Protein-protein interaction databases

STRINGi226186.BT_3812

Structurei

3D structure databases

ProteinModelPortaliQ8A155
SMRiQ8A155
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 149MGS-likePROSITE-ProRule annotationAdd BLAST149

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
InParanoidiQ8A155
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
PROSITEiView protein in PROSITE
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q8A155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESKRIKTA LVSVYHKEGL DEIITKLYEE GVEFLSTGGT RQFIESLGYP
60 70 80 90 100
CKAVEDLTTY PSILGGRVKT LHPKIFGGIL CRRDLEQDIQ QIEKYEIPEI
110 120 130 140 150
DLVIVDLYPF EATVASGASE ADIIEKIDIG GISLIRAAAK NYNDVIIVAS
160 170 180 190 200
QAQYKPLLDM LMEHGATSSL EERRWMAKEA FAVSSHYDSA IFNYFDAGEG
210 220 230 240 250
SAFRCSVNNQ KQLRYGENPH QKGYFYGNLD AMFDQIHGKE ISYNNLLDIN
260 270 280 290 300
AAVDLIDEYE DLTFAILKHN NACGLASRPT VLEAWTDALA GDPVSAFGGV
310 320 330 340 350
LITNGVIDKA AAEEINKIFF EVIIAPDYDV DALEILGQKK NRIILVRKEA
360 370 380 390 400
KLPKKQFRAL LNGVLVQDKD MNIETVADLR TVTDKAPTPE EVEDLLFANK
410 420 430 440 450
IVKNSKSNAI VLAKGKQLLA SGVGQTSRVD ALKQAIEKAK SFGFDLNGAV
460 470 480 490 500
MASDAFFPFP DCVEIADKEG ITAVIQPGGS VKDDLTFAYC NEHGMAMVTT

GIRHFKH
Length:507
Mass (Da):55,880
Last modified:June 20, 2003 - v1
Checksum:i0C09966527E570E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA Translation: AAO78917.1
RefSeqiNP_812723.1, NC_004663.1
WP_008762746.1, NC_004663.1

Genome annotation databases

EnsemblBacteriaiAAO78917; AAO78917; BT_3812
GeneIDi1072684
31618879
KEGGibth:BT_3812
PATRICifig|226186.12.peg.3876

Similar proteinsi

Entry informationi

Entry nameiPUR9_BACTN
AccessioniPrimary (citable) accession number: Q8A155
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: May 23, 2018
This is version 91 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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