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Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208ATP phosphoribosyltransferasePRO_0000151944Add
BLAST

Interactioni

Subunit structurei

Heteromultimer composed of HisG and HisZ subunits.By similarity

Protein-protein interaction databases

STRINGi243274.TM1042.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi12 – 2211Combined sources
Beta strandi26 – 294Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 446Combined sources
Helixi46 – 483Combined sources
Helixi49 – 546Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 706Combined sources
Beta strandi79 – 9315Combined sources
Turni94 – 963Combined sources
Beta strandi103 – 1086Combined sources
Helixi110 – 11910Combined sources
Beta strandi124 – 1285Combined sources
Helixi135 – 1384Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 15210Combined sources
Helixi153 – 1575Combined sources
Beta strandi160 – 17516Combined sources
Helixi177 – 1826Combined sources
Helixi184 – 20320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O63X-ray2.00A/B2-208[»]
1O64X-ray2.10A/B2-208[»]
1USYX-ray2.52E/F/G/H1-208[»]
ProteinModelPortaliQ9X0D2.
SMRiQ9X0D2. Positions 1-203.
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.
OMAiVIIVRAT.

Family and domain databases

CDDicd13595. PBP2_HisGs. 1 hit.
HAMAPiMF_01018. HisG_Short. 1 hit.
InterProiIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR024893. ATP_PRibTrfase_HisG_short.
[Graphical view]
PANTHERiPTHR21403. PTHR21403. 1 hit.
PTHR21403:SF3. PTHR21403:SF3. 1 hit.
PfamiPF01634. HisG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00070. hisG. 1 hit.
PROSITEiPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]

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.
tmi:THEMA_09150.
tmw:THMA_1064.
PATRICi23937013. VBITheMar51294_1055.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O63X-ray2.00A/B2-208[»]
1O64X-ray2.10A/B2-208[»]
1USYX-ray2.52E/F/G/H1-208[»]
ProteinModelPortaliQ9X0D2.
SMRiQ9X0D2. Positions 1-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36119; AAD36119; TM_1042.
GeneIDi898709.
KEGGitma:TM1042.
tmi:THEMA_09150.
tmw:THMA_1064.
PATRICi23937013. VBITheMar51294_1055.

Phylogenomic databases

eggNOGiENOG4105E21. Bacteria.
COG0040. LUCA.
InParanoidiQ9X0D2.
KOiK00765.
OMAiVIIVRAT.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.

Miscellaneous databases

EvolutionaryTraceiQ9X0D2.

Family and domain databases

CDDicd13595. PBP2_HisGs. 1 hit.
HAMAPiMF_01018. HisG_Short. 1 hit.
InterProiIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR024893. ATP_PRibTrfase_HisG_short.
[Graphical view]
PANTHERiPTHR21403. PTHR21403. 1 hit.
PTHR21403:SF3. PTHR21403:SF3. 1 hit.
PfamiPF01634. HisG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00070. hisG. 1 hit.
PROSITEiPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS1_THEMA
AccessioniPrimary (citable) accession number: Q9X0D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 122 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.