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Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Cofactori

Mg2+By similarity

Enzyme regulationi

Feedback inhibited by histidine.By similarity

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)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. 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, Magnesium, Metal-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:MTH_1506
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001518861 – 287ATP phosphoribosyltransferaseAdd BLAST287

Interactioni

Protein-protein interaction databases

STRINGi187420.MTH1506.

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi14 – 23Combined sources10
Beta strandi28 – 30Combined sources3
Beta strandi36 – 42Combined sources7
Beta strandi45 – 50Combined sources6
Turni52 – 54Combined sources3
Helixi55 – 60Combined sources6
Beta strandi63 – 70Combined sources8
Helixi71 – 77Combined sources7
Beta strandi82 – 86Combined sources5
Beta strandi92 – 99Combined sources8
Helixi107 – 109Combined sources3
Beta strandi115 – 119Combined sources5
Helixi121 – 130Combined sources10
Beta strandi136 – 139Combined sources4
Helixi144 – 146Combined sources3
Turni147 – 151Combined sources5
Beta strandi154 – 162Combined sources9
Helixi164 – 168Combined sources5
Beta strandi171 – 180Combined sources10
Beta strandi182 – 186Combined sources5
Helixi188 – 193Combined sources6
Helixi195 – 210Combined sources16
Turni211 – 213Combined sources3
Beta strandi214 – 222Combined sources9
Helixi223 – 225Combined sources3
Helixi226 – 232Combined sources7
Beta strandi236 – 238Combined sources3
Beta strandi240 – 243Combined sources4
Beta strandi246 – 248Combined sources3
Beta strandi250 – 258Combined sources9
Turni259 – 261Combined sources3
Helixi262 – 270Combined sources9
Turni271 – 273Combined sources3
Beta strandi275 – 281Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VD3X-ray2.45A/B2-287[»]
ProteinModelPortaliO27550.
SMRiO27550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO27550.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG02208. Archaea.
COG0040. LUCA.
KOiK00765.
OMAiYVMMDYD.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long. 1 hit.
InterProiIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]
PANTHERiPTHR21403. PTHR21403. 1 hit.
PfamiPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
TIGRFAMsiTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEiPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O27550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIRIAVPSK GRISEPAIRL LENAGVGLKD TVNRKLFSKT QHPQIEVMFS
60 70 80 90 100
RAADIPEFVA DGAADLGITG YDLIVERGSD VEILEDLKYG RASLVLAAPE
110 120 130 140 150
DSTIRGPEDI PRGAVIATEF PGITENYLRE HGIDAEVVEL TGSTEIAPFI
160 170 180 190 200
GVADLITDLS STGTTLRMNH LRVIDTILES SVKLIANRES YATKSGIIEE
210 220 230 240 250
LRTGIRGVID AEGKRLVMLN IDRKNLDRVR ALMPGMTGPT VSEVLSDNGV
260 270 280
VAVHAVVDEK EVFNLINRLK AVGARDILVV PIERIIP
Length:287
Mass (Da):31,165
Last modified:January 1, 1998 - v1
Checksum:iEFAA5D8BF9755F48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85981.1.
PIRiH69067.
RefSeqiWP_010877116.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85981; AAB85981; MTH_1506.
GeneIDi1471775.
KEGGimth:MTH_1506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85981.1.
PIRiH69067.
RefSeqiWP_010877116.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VD3X-ray2.45A/B2-287[»]
ProteinModelPortaliO27550.
SMRiO27550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH1506.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85981; AAB85981; MTH_1506.
GeneIDi1471775.
KEGGimth:MTH_1506.

Phylogenomic databases

eggNOGiarCOG02208. Archaea.
COG0040. LUCA.
KOiK00765.
OMAiYVMMDYD.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.

Miscellaneous databases

EvolutionaryTraceiO27550.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long. 1 hit.
InterProiIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]
PANTHERiPTHR21403. PTHR21403. 1 hit.
PfamiPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
TIGRFAMsiTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEiPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS1_METTH
AccessioniPrimary (citable) accession number: O27550
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 112 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.