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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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), 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), 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

BRENDAi3.5.4.10 6331
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:TM_1249
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001921421 – 452Bifunctional purine biosynthesis protein PurHAdd BLAST452

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1249

Structurei

Secondary structure

1452
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi27 – 30Combined sources4
Helixi32 – 40Combined sources9
Helixi48 – 51Combined sources4
Helixi57 – 60Combined sources4
Turni61 – 64Combined sources4
Helixi67 – 74Combined sources8
Beta strandi75 – 77Combined sources3
Beta strandi81 – 85Combined sources5
Helixi96 – 106Combined sources11
Turni107 – 110Combined sources4
Beta strandi112 – 114Combined sources3
Helixi117 – 125Combined sources9
Helixi129 – 154Combined sources26
Beta strandi158 – 165Combined sources8
Beta strandi172 – 174Combined sources3
Beta strandi179 – 183Combined sources5
Beta strandi186 – 190Combined sources5
Beta strandi192 – 194Combined sources3
Helixi198 – 212Combined sources15
Beta strandi215 – 223Combined sources9
Beta strandi226 – 232Combined sources7
Helixi236 – 246Combined sources11
Turni247 – 253Combined sources7
Beta strandi254 – 260Combined sources7
Helixi264 – 269Combined sources6
Beta strandi274 – 278Combined sources5
Helixi284 – 290Combined sources7
Beta strandi296 – 300Combined sources5
Beta strandi306 – 311Combined sources6
Beta strandi314 – 319Combined sources6
Beta strandi328 – 332Combined sources5
Helixi337 – 352Combined sources16
Beta strandi358 – 362Combined sources5
Beta strandi365 – 370Combined sources6
Helixi376 – 387Combined sources12
Helixi388 – 391Combined sources4
Beta strandi395 – 400Combined sources6
Helixi405 – 413Combined sources9
Beta strandi418 – 421Combined sources4
Helixi428 – 438Combined sources11
Beta strandi441 – 444Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCZX-ray1.88A/B1-452[»]
ProteinModelPortaliQ9X0X6
SMRiQ9X0X6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0X6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 115MGS-likePROSITE-ProRule annotationAdd BLAST115

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105DC1 Bacteria
COG0138 LUCA
InParanoidiQ9X0X6
KOiK00602
OMAiDLLFAWK

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.

Q9X0X6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRILVSLYE KEKYLDILRE LHEKGWEIWA SSGTAKFLKS NGIEANDVST
60 70 80 90 100
ITGFENLLGG LVKTLHPEIF AGILGPEPRW DVVFVDLYPP PDIDIGGVAL
110 120 130 140 150
LRAAAKNWKK VKPAFDMETL KLAIEIDDEE TRKYLAGMTF AFTSVYDSIR
160 170 180 190 200
ANQFVEGISL AFKREDLQLR YGENPHEKAF VYGKPAFEIL HEGKTISFNN
210 220 230 240 250
ILDAENAWFM AKNLPRMGAV VVKHQSPCGA AIGEDKVEIV KKAIEADDES
260 270 280 290 300
SFGGILAVNF EMDEEVAKSL KKYLEVIVAP SFTQEAIEVL SKKKVRLLKP
310 320 330 340 350
GDYASWAGKM AFGSLVLSER KYPEGNFELV VGEPLSEKEL EDLEFAYRVV
360 370 380 390 400
EGAKSNAVLI AKDGVTVGIG SGQPSRKRAA WIATVMAGEK AKGAVAASDA
410 420 430 440 450
FFPFPDSLEI LAQAGVKAVV APLGSIRDEE VIEKARELGI TFYKAPSRVF

RH
Length:452
Mass (Da):49,867
Last modified:November 1, 1999 - v1
Checksum:iE4537EF51A5C4469
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA Translation: AAD36324.1
PIRiC72277
RefSeqiNP_229054.1, NC_000853.1
WP_004080014.1, NZ_CP011107.1

Genome annotation databases

EnsemblBacteriaiAAD36324; AAD36324; TM_1249
GeneIDi29651998
898234
KEGGitma:TM1249

Similar proteinsi

Entry informationi

Entry nameiPUR9_THEMA
AccessioniPrimary (citable) accession number: Q9X0X6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 28, 2018
This is version 125 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health