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Protein

ATP phosphoribosyltransferase

Gene

hisG

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

Functioni

Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).By similarity

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathwayi: L-histidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Probable histidinol-phosphatase (hisK)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006

Names & Taxonomyi

Protein namesi
Recommended name:
ATP phosphoribosyltransferase (EC:2.4.2.17)
Short name:
ATP-PRT
Short name:
ATP-PRTase
Gene namesi
Name:hisG
Ordered Locus Names:TM_1042
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001519441 – 208ATP phosphoribosyltransferaseAdd BLAST208

Interactioni

Subunit structurei

Heteromultimer composed of HisG and HisZ subunits.By similarity

Protein-protein interaction databases

STRINGi243274.TM1042

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi12 – 22Combined sources11
Beta strandi26 – 29Combined sources4
Beta strandi31 – 36Combined sources6
Beta strandi39 – 44Combined sources6
Helixi46 – 48Combined sources3
Helixi49 – 54Combined sources6
Beta strandi59 – 64Combined sources6
Helixi65 – 70Combined sources6
Beta strandi79 – 93Combined sources15
Turni94 – 96Combined sources3
Beta strandi103 – 108Combined sources6
Helixi110 – 119Combined sources10
Beta strandi124 – 128Combined sources5
Helixi135 – 138Combined sources4
Beta strandi139 – 141Combined sources3
Beta strandi143 – 152Combined sources10
Helixi153 – 157Combined sources5
Beta strandi160 – 175Combined sources16
Helixi177 – 182Combined sources6
Helixi184 – 203Combined sources20

3D structure databases

ProteinModelPortaliQ9X0D2
SMRiQ9X0D2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0D2

Family & Domainsi

Domaini

Lacks the C-terminal regulatory region which is replaced by HisZ.

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E21 Bacteria
COG0040 LUCA
InParanoidiQ9X0D2
KOiK00765
OMAiYVMMDYD

Family and domain databases

CDDicd13595 PBP2_HisGs, 1 hit
HAMAPiMF_01018 HisG_Short, 1 hit
InterProiView protein in InterPro
IPR013820 ATP_PRibTrfase_cat
IPR018198 ATP_PRibTrfase_CS
IPR001348 ATP_PRibTrfase_HisG
IPR024893 ATP_PRibTrfase_HisG_short
PANTHERiPTHR21403 PTHR21403, 1 hit
PfamiView protein in Pfam
PF01634 HisG, 1 hit
TIGRFAMsiTIGR00070 hisG, 1 hit
PROSITEiView protein in PROSITE
PS01316 ATP_P_PHORIBOSYLTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q9X0D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLAIPKGR LEEKVMTYLK KTGVIFERES SILREGKDIV CFMVRPFDVP
60 70 80 90 100
TYLVHGVADI GFCGTDVLLE KETSLIQPFF IPTNISRMVL AGPKGRGIPE
110 120 130 140 150
GEKRIATKFP NVTQRYCESK GWHCRIIPLK GSVELAPIAG LSDLIVDITE
160 170 180 190 200
TGRTLKENNL EILDEIFVIR THVVVNPVSY RTKREEVVSF LEKLQEVIEH

DSNEQSRG
Length:208
Mass (Da):23,511
Last modified:November 1, 1999 - v1
Checksum:iA3629EF262F48A80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA Translation: AAD36119.1
PIRiA72305
RefSeqiNP_228848.1, NC_000853.1
WP_004080478.1, NZ_CP011107.1

Genome annotation databases

EnsemblBacteriaiAAD36119; AAD36119; TM_1042
GeneIDi898709
KEGGitma:TM1042

Similar proteinsi

Entry informationi

Entry nameiHIS1_THEMA
AccessioniPrimary (citable) accession number: Q9X0D2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 7, 2017
This is version 127 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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