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
Acaryochloris marina (strain MBIC 11017)
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

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:AM1_5779
OrganismiAcaryochloris marina (strain MBIC 11017)
Taxonomic identifieri329726 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesAcaryochloridaceaeAcaryochloris
Proteomesi
  • UP000000268 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000764721 – 524Bifunctional purine biosynthesis protein PurHAdd BLAST524

Proteomic databases

PRIDEiB0BZH9

Interactioni

Protein-protein interaction databases

STRINGi329726.AM1_5779

Structurei

3D structure databases

ProteinModelPortaliB0BZH9
SMRiB0BZH9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 154MGS-likePROSITE-ProRule annotationAdd BLAST154

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.

B0BZH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLALLSTS DKTGLVELAQ QLVNEYGFTL VSSGGTAVTI EKAGLPVTKV
60 70 80 90 100
SDYTGSPEIL GGRVKTLHPR IHGGILARRS LESDVQDLTE NNIQGIDLVV
110 120 130 140 150
VNLYPFEETI AKQKAQGITD PDQALADAVE QIDIGGPTMI RAAAKNHAHV
160 170 180 190 200
TVLCDPQQYA SYLQELKHGE GETSLPFRQA CALKVFERMA SYDRAIATHL
210 220 230 240 250
RQSLATTDSQ TQLSILGTAK QTLRYGENPH QNAVWYQESD TASGWAAAQQ
260 270 280 290 300
LQGKELSYNN LVDLEAARRV IAEFAQAETQ PTVAILKHNN PCGVAQGETL
310 320 330 340 350
LQAYEKALAA DSVSAFGGIV AMNRAIDTDT AQVLTKTFLE CIVAPECQPE
360 370 380 390 400
AAAVLQAKSN LRVLVLPDLV SGPAVTVKAI AGGWLAQAAD ETLTPPADWQ
410 420 430 440 450
IVTQAKPTEA QLAELLFAWK VVKHVKSNAI VVTKDHTTLG VGAGQMNRVG
460 470 480 490 500
SVNIALQQAG EKAQGGTLAS DGFFPFDDSV RTAAAAGITA IIQPGGSIRD
510 520
KDSIQAADEL GIVMAFTGTR HFLH
Length:524
Mass (Da):55,848
Last modified:February 26, 2008 - v1
Checksum:iE979D0DFD30BA415
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000828 Genomic DNA Translation: ABW30724.1
RefSeqiWP_012165938.1, NC_009925.1

Genome annotation databases

EnsemblBacteriaiABW30724; ABW30724; AM1_5779
KEGGiamr:AM1_5779

Similar proteinsi

Entry informationi

Entry nameiPUR9_ACAM1
AccessioniPrimary (citable) accession number: B0BZH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: March 28, 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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health