Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Methanothermobacter sp. CaT2
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Feedback inhibited by histidine.UniRule annotation

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.UniRule annotation
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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

Keywordsi

Molecular functionGlycosyltransferaseUniRule annotationImported, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesisUniRule annotation
LigandATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP phosphoribosyltransferaseUniRule annotation (EC:2.4.2.17UniRule annotation)
Short name:
ATP-PRTUniRule annotation
Short name:
ATP-PRTaseUniRule annotation
Gene namesi
Name:hisGUniRule annotation
ORF Names:MTCT_1369Imported
OrganismiMethanothermobacter sp. CaT2Imported
Taxonomic identifieri866790 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000031654 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 207HisGInterPro annotationAdd BLAST157
Domaini211 – 284HisG_CInterPro annotationAdd BLAST74

Sequence similaritiesi

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.UniRule annotation

Phylogenomic databases

KOiK00765.
OrthoDBiPOG093Z06DC.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long. 1 hit.
InterProiView protein in InterPro
IPR013820. 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.
PANTHERiPTHR21403. PTHR21403. 1 hit.
PfamiView protein in Pfam
PF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
SUPFAMiSSF54913. SSF54913. 1 hit.
TIGRFAMsiTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEiView protein in PROSITE
PS01316. ATP_P_PHORIBOSYLTR. 1 hit.

Sequencei

Sequence statusi: Complete.

T2GJK2-1 [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 PQGAVIATEF 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):31,137
Last modified:November 13, 2013 - v1
Checksum:iE4C6A1754DE71424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011952 Genomic DNA. Translation: BAM70617.1.
RefSeqiWP_048176022.1. NZ_AP011952.1.

Genome annotation databases

EnsemblBacteriaiBAM70617; BAM70617; MTCT_1369.
GeneIDi24854611.
KEGGimetc:MTCT_1369.

Similar proteinsi

Entry informationi

Entry nameiT2GJK2_9EURY
AccessioniPrimary (citable) accession number: T2GJK2
Entry historyiIntegrated into UniProtKB/TrEMBL: November 13, 2013
Last sequence update: November 13, 2013
Last modified: September 27, 2017
This is version 20 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported