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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
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

BioCyciOANT439375:G1G9F-1142-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:Oant_1087
OrganismiOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Taxonomic identifieri439375 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
Proteomesi
  • UP000002301 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000189201 – 538Bifunctional purine biosynthesis protein PurHAdd BLAST538

Proteomic databases

PRIDEiA6WXV3

Interactioni

Protein-protein interaction databases

STRINGi439375.Oant_1087

Structurei

3D structure databases

ProteinModelPortaliA6WXV3
SMRiA6WXV3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 158MGS-likePROSITE-ProRule annotationAdd BLAST153

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
HOGENOMiHOG000230372
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.

A6WXV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSSKHIPA PDLHRVRRAL LSVSDKTGLI DFAKALHAQG VEILSTGGTA
60 70 80 90 100
KSIAAEGIPV KDVSEVTGFP EIMDGRVKTL HPAVHGGLLA VRNDREHVAA
110 120 130 140 150
MEEHGIGGID LAVINLYPFE EVRFKGGDYD TTVENIDIGG PAMIRASAKN
160 170 180 190 200
HAYVATVVDP ADYADVVAEL EKHAGSLPLA FRKKLAAKAF SRTAAYDAAI
210 220 230 240 250
SNWFAEAINE ETPVYRSVAG KLHSVMRYGE NPHQTAGFYL TGEKRPGVAT
260 270 280 290 300
ATQLQGKQLS YNNINDTDAA FELVAEFDPA RTAAVAIIKH ANPCGVAEAA
310 320 330 340 350
TIKEAYLKAL ACDPVSAFGG IVALNKTLDE EAAEEIVKIF TEVIIAPDAT
360 370 380 390 400
EGAQAIVAAK KNLRLLVTGG LPDPRAKGIA AKTVAGGLLV QSRDNGVVDD
410 420 430 440 450
LDLKVVTKRA PTEAELNDMK FAFRVGKHVK SNAIVYVKDG ATVGIGAGQM
460 470 480 490 500
SRVDSARIAA RKAEDAAEAA GLAEPLTKGC VVASDAFFPF ADGLLSAVQA
510 520 530
GATAVIQPGG SMRDDEVIAA ADEHGIAMVM TGMRHFRH
Length:538
Mass (Da):56,639
Last modified:August 21, 2007 - v1
Checksum:iF6795E5CE7E7095B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000758 Genomic DNA Translation: ABS13807.1
RefSeqiWP_012091248.1, NC_009667.1

Genome annotation databases

EnsemblBacteriaiABS13807; ABS13807; Oant_1087
GeneIDi5379484
KEGGioan:Oant_1087
PATRICifig|439375.7.peg.1136

Similar proteinsi

Entry informationi

Entry nameiPUR9_OCHA4
AccessioniPrimary (citable) accession number: A6WXV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 23, 2018
This is version 68 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
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Main funding by: National Institutes of Health