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Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
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.

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 regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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. Histidinol-phosphatase (hisK)
  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, Nucleotide-binding

Enzyme and pathway databases

BioCyciLLAC272623:GHSH-1295-MONOMER.
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:LL1208
ORF Names:L0066
OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifieri272623 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000002196 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_0000151911Add
BLAST

Proteomic databases

PaxDbiQ02129.

Interactioni

Subunit structurei

Heterooctamer composed of four HisG and four HisZ subunits.1 Publication

Protein-protein interaction databases

STRINGi272623.L0066.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi10 – 2011Combined sources
Turni21 – 233Combined sources
Beta strandi36 – 383Combined sources
Beta strandi46 – 494Combined sources
Helixi51 – 599Combined sources
Beta strandi64 – 696Combined sources
Helixi70 – 756Combined sources
Beta strandi81 – 877Combined sources
Beta strandi93 – 986Combined sources
Helixi100 – 1045Combined sources
Beta strandi111 – 1166Combined sources
Helixi118 – 12710Combined sources
Beta strandi132 – 1365Combined sources
Helixi143 – 1464Combined sources
Beta strandi151 – 16010Combined sources
Helixi161 – 1644Combined sources
Turni165 – 1673Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi179 – 1846Combined sources
Helixi185 – 20218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7MX-ray2.90E/F/G/H1-208[»]
1Z7NX-ray3.25E/F/G/H1-208[»]
ProteinModelPortaliQ02129.
SMRiQ02129. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02129.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E21. Bacteria.
COG0040. LUCA.
HOGENOMiHOG000223248.
KOiK00765.
OrthoDBiEOG66MQT3.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q02129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKIAITKGR IQKQVTKLLE NADYDVEPIL NLGRELQIKT KDDLQIIFGK
60 70 80 90 100
PNDVITFLEH GIVDIGFVGK DTLDENDFDD YYELLYLKIG QCIFALASYP
110 120 130 140 150
DFSNKNFQRH KRIASKYPRV TKKYFAQKQE DIEIIKLEGS VELGPVVGLA
160 170 180 190 200
DAIVDIVETG NTLSANGLEV IEKISDISTR MIVNKSSFKF KKDKIIEMVE

RLEDAQTN
Length:208
Mass (Da):23,677
Last modified:September 26, 2001 - v2
Checksum:i8CE4CD0A16D39FEF
GO

Sequence cautioni

The sequence AAK05306.1 differs from that shown. Reason: Frameshift at position 174. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511P → A in AAB81903 (PubMed:1400209).Curated
Sequence conflicti86 – 861Y → D in AAB81903 (PubMed:1400209).Curated
Sequence conflicti110 – 1101H → R in AAB81903 (PubMed:1400209).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92974 Genomic DNA. Translation: AAB81903.1.
AE005176 Genomic DNA. Translation: AAK05306.1. Frameshift.
PIRiD45734.
H86775.
RefSeqiNP_267364.1. NC_002662.1.

Genome annotation databases

EnsemblBacteriaiAAK05306; AAK05306; L0066.
GeneIDi1114855.
KEGGilla:L0066.
PATRICi22294790. VBILacLac136773_1303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92974 Genomic DNA. Translation: AAB81903.1.
AE005176 Genomic DNA. Translation: AAK05306.1. Frameshift.
PIRiD45734.
H86775.
RefSeqiNP_267364.1. NC_002662.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7MX-ray2.90E/F/G/H1-208[»]
1Z7NX-ray3.25E/F/G/H1-208[»]
ProteinModelPortaliQ02129.
SMRiQ02129. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272623.L0066.

Proteomic databases

PaxDbiQ02129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK05306; AAK05306; L0066.
GeneIDi1114855.
KEGGilla:L0066.
PATRICi22294790. VBILacLac136773_1303.

Phylogenomic databases

eggNOGiENOG4105E21. Bacteria.
COG0040. LUCA.
HOGENOMiHOG000223248.
KOiK00765.
OrthoDBiEOG66MQT3.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.
BioCyciLLAC272623:GHSH-1295-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02129.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis."
    Delorme C., Ehrlich S.D., Renault P.
    J. Bacteriol. 174:6571-6579(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCDO 2118.
  2. "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
    Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
    Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IL1403.
  3. "An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis."
    Sissler M., Delorme C., Bond J., Ehrlich S.D., Renault P., Francklyn C.
    Proc. Natl. Acad. Sci. U.S.A. 96:8985-8990(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP transferase from Lactococcus lactis."
    Bovee M.L., Champagne K.S., Demeler B., Francklyn C.S.
    Biochemistry 41:11838-11846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiHIS1_LACLA
AccessioniPrimary (citable) accession number: Q02129
Secondary accession number(s): Q9CG94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 26, 2001
Last modified: May 11, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The stability and homogeneity of the HisG-HisZ complex is apparently increased by ATP and 5-phosphoribose 1-diphosphate but decreased in the presence of the regulatory inhibitor histidine.

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.