Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Prochlorococcus marinus (strain MIT 9515)
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

BioCyciPMAR167542:G1G7Y-296-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:P9515_02991
OrganismiProchlorococcus marinus (strain MIT 9515)
Taxonomic identifieri167542 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001589 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000189281 – 517Bifunctional purine biosynthesis protein PurHAdd BLAST517

Interactioni

Protein-protein interaction databases

STRINGi167542.P9515_02991

Structurei

3D structure databases

ProteinModelPortaliA2BUP7
SMRiA2BUP7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 145MGS-likePROSITE-ProRule annotationAdd BLAST145

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.

A2BUP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPLALVSVS DKTNIIPFCK DLVEKFGYNI LSSGGTAEYL TEAKVPVLKV
60 70 80 90 100
ADFTESPEIL DGRVKTLHPK IHGGILAKRS NEEHQREILE NKLELIDLVV
110 120 130 140 150
VNLYPFKKKV EEQCPWEEAI ENIDIGGPSM IRSAAKNHAD VAVLVDPNQY
160 170 180 190 200
QNYIEEIKKG PLSKDFKTKL AFEAFQHTAS YDSAISNWIS KEKDLRPSNF
210 220 230 240 250
IESYPLIKQL RYGENPHQKA LWYGLNNIGW NSAEQLQGKE LSYNNILDLE
260 270 280 290 300
SALLTVLEFG YETKPNIKTE SIAAVILKHN NPCGASISNS ASSSFKNALK
310 320 330 340 350
CDSVSAFGGI VAFNANVDKE TALILKDIFL ECVVAPSFDK EALEIFKTKK
360 370 380 390 400
NLRVLKLTKE MLPKENQTCS KSIMGGILIQ DSDNQENSED SWISVTKKNP
410 420 430 440 450
TEQEYLDLKF AWKICKHVKS NAIVVAKDQQ TLGIGAGQMN RVGASKIALE
460 470 480 490 500
AAKEIDSGGV LASDGFFPFA DTVRLADKYG ISSIIQPGGS IRDEESIKMC
510
DSRGISMIFT HKRHFLH
Length:517
Mass (Da):57,437
Last modified:February 20, 2007 - v1
Checksum:iAE9C2D43313409ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA Translation: ABM71508.1
RefSeqiWP_011819618.1, NC_008817.1

Genome annotation databases

EnsemblBacteriaiABM71508; ABM71508; P9515_02991
KEGGipmc:P9515_02991

Similar proteinsi

Entry informationi

Entry nameiPUR9_PROM5
AccessioniPrimary (citable) accession number: A2BUP7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: March 28, 2018
This is version 70 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health