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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331)
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

BioCyciCSAC351627:G1G8P-2047-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:Csac_1992
OrganismiCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331)
Taxonomic identifieri351627 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
Proteomesi
  • UP000000256 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000188661 – 513Bifunctional purine biosynthesis protein PurHAdd BLAST513

Proteomic databases

PRIDEiA4XKZ2

Interactioni

Protein-protein interaction databases

STRINGi351627.Csac_1992

Structurei

3D structure databases

ProteinModelPortaliA4XKZ2
SMRiA4XKZ2
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.

A4XKZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKAIISVY NKDGILEFAK ELKNLGYEII STGGTMKYLK ENRIDVINIS
60 70 80 90 100
DVTNFPEILD GRVKTLHPNI HAGILAIKDN EEHVKTLNDL NISTIDMVVV
110 120 130 140 150
NLYPFKETIF RENVAFEDVI ENIDIGGPTM LRAAAKNFKY ITVIIDPADY
160 170 180 190 200
GLVLKEIKEN GDVSFETRFY LATKVFEYTA YYDSMIFNYF KYIRGDKSFP
210 220 230 240 250
DYLTVPLETV QKLRYGENPH QQASFYKITL PFIEKSNIAN AEQLHGKDLS
260 270 280 290 300
YNNILDSDSA IELLKEFDEP TCVAIKHNNP CGVASGDNIF EAYKKVYNSD
310 320 330 340 350
PVSIFGGIVA FNRKVDRQTA EELKKIFLEI VIAPDFDEDA LSLLSTKKDL
360 370 380 390 400
RILKLLTLDK TDVYYDVKSV NGGMLVQEKD RKLLNEDYQV VTERRPTEKE
410 420 430 440 450
IEDLIFAWKV VKHVKSNAIV IAKDKMTLGI GMGQTNRIWA VEHAISRSRF
460 470 480 490 500
DLNGAVLASD AFFPFSDSVE AAGKAGITAI IQPGGSIRDK ESIDAANKYN
510
IAMIFTGIRH FRH
Length:513
Mass (Da):58,028
Last modified:May 29, 2007 - v1
Checksum:iD217E2C207CBC537
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000679 Genomic DNA Translation: ABP67577.1
RefSeqiWP_011917512.1, NC_009437.1

Genome annotation databases

EnsemblBacteriaiABP67577; ABP67577; Csac_1992
KEGGicsc:Csac_1992

Similar proteinsi

Entry informationi

Entry nameiPUR9_CALS8
AccessioniPrimary (citable) accession number: A4XKZ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: May 23, 2018
This is version 66 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

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