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Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Campylobacter jejuni (strain RM1221)
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.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. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  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

BioCyciCJEJ195099:GJC0-1799-MONOMER.
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
Ordered Locus Names:CJE1769
OrganismiCampylobacter jejuni (strain RM1221)
Taxonomic identifieri195099 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299ATP phosphoribosyltransferasePRO_0000151840Add
BLAST

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510Combined sources
Helixi16 – 2712Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 5310Combined sources
Helixi55 – 573Combined sources
Helixi58 – 636Combined sources
Beta strandi66 – 738Combined sources
Helixi74 – 8613Combined sources
Beta strandi93 – 986Combined sources
Beta strandi104 – 1118Combined sources
Helixi119 – 1224Combined sources
Beta strandi126 – 1305Combined sources
Helixi132 – 14110Combined sources
Beta strandi147 – 1504Combined sources
Helixi155 – 1573Combined sources
Turni158 – 1625Combined sources
Beta strandi165 – 17410Combined sources
Helixi175 – 1795Combined sources
Beta strandi182 – 19110Combined sources
Beta strandi193 – 2008Combined sources
Helixi204 – 22320Combined sources
Beta strandi226 – 2349Combined sources
Helixi235 – 2373Combined sources
Helixi238 – 2447Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi259 – 27012Combined sources
Helixi271 – 28313Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi295 – 2984Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YB5X-ray2.24A/B/C/D/E/F1-299[»]
4YB6X-ray1.98A/B/C/D/E/F1-299[»]
4YB7X-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-299[»]
ProteinModelPortaliQ5HSJ4.
SMRiQ5HSJ4. Positions 5-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000223247.
KOiK00765.
OMAiCDIVSSG.
OrthoDBiEOG66MQT3.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long.
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.

Q5HSJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQENTRLRIA IQKSGRLSKE SIELLSECGV KMHIHEQSLI AFSTNLPIDI
60 70 80 90 100
LRVRDDDIPG LIFDGVVDLG IIGENVLEEN ELERQSLGEN PSYKLLKKLD
110 120 130 140 150
FGYCRLSLAL PQENKFQNLK DFEGLRIATS YPQLLKRFMK ENGINYKNCT
160 170 180 190 200
LTGSVEVAPR ANLADAICDL VSSGATLQAN NLKEVKVIYE SRACLIQKEN
210 220 230 240 250
ALSKEKQALV DKIMLRVAGV MQARESKYIM LHAPKEKLDK IQALLPGVER
260 270 280 290
PTILPLAHDE KNVALHMVSK ENLFWETMEA LKEEGASSIL VLPIEKMLK
Length:299
Mass (Da):33,639
Last modified:February 15, 2005 - v1
Checksum:i9362C62019697F4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000025 Genomic DNA. Translation: AAW36193.1.
RefSeqiWP_002858407.1. NC_003912.7.

Genome annotation databases

EnsemblBacteriaiAAW36193; AAW36193; CJE1769.
KEGGicjr:CJE1769.
PATRICi20045348. VBICamJej134361_1785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000025 Genomic DNA. Translation: AAW36193.1.
RefSeqiWP_002858407.1. NC_003912.7.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YB5X-ray2.24A/B/C/D/E/F1-299[»]
4YB6X-ray1.98A/B/C/D/E/F1-299[»]
4YB7X-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-299[»]
ProteinModelPortaliQ5HSJ4.
SMRiQ5HSJ4. Positions 5-299.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW36193; AAW36193; CJE1769.
KEGGicjr:CJE1769.
PATRICi20045348. VBICamJej134361_1785.

Phylogenomic databases

HOGENOMiHOG000223247.
KOiK00765.
OMAiCDIVSSG.
OrthoDBiEOG66MQT3.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.
BioCyciCJEJ195099:GJC0-1799-MONOMER.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM1221.

Entry informationi

Entry nameiHIS1_CAMJR
AccessioniPrimary (citable) accession number: Q5HSJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 15, 2005
Last modified: June 8, 2016
This is version 81 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

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.