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Q02129 (HIS1_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP phosphoribosyltransferase

Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17
Gene names
Name:hisG
Ordered Locus Names:LL1208
ORF Names:L0066
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP MF_01018

Catalytic activity

1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01018

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_01018

Subunit structure

Heterooctamer composed of four hisG and four hisZ subunits Probable. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP MF_01018.

Domain

Lacks the C-terminal regulatory region which is replaced by hisZ. HAMAP MF_01018

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. HAMAP MF_01018

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Short subfamily.

Sequence caution

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP phosphoribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208ATP phosphoribosyltransferase HAMAP MF_01018
PRO_0000151911

Experimental info

Sequence conflict511P → A in AAB81903. Ref.1
Sequence conflict861Y → D in AAB81903. Ref.1
Sequence conflict1101H → R in AAB81903. Ref.1

Secondary structure

...................................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02129 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 8CE4CD0A16D39FEF

FASTA20823,677
        10         20         30         40         50         60 
MIKIAITKGR IQKQVTKLLE NADYDVEPIL NLGRELQIKT KDDLQIIFGK PNDVITFLEH 

        70         80         90        100        110        120 
GIVDIGFVGK DTLDENDFDD YYELLYLKIG QCIFALASYP DFSNKNFQRH KRIASKYPRV 

       130        140        150        160        170        180 
TKKYFAQKQE DIEIIKLEGS VELGPVVGLA DAIVDIVETG NTLSANGLEV IEKISDISTR 

       190        200 
MIVNKSSFKF KKDKIIEMVE RLEDAQTN 

« Hide

References

« Hide 'large scale' references
[1]"Histidine biosynthesis genes in Lactococcus lactis subsp. lactis."
Delorme C., Ehrlich S.D., Renault P.
J. Bacteriol. 174:6571-6579(1992) [PubMed: 1400209] [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: 11337471] [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: 10430882] [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: 12269828] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92974 Genomic DNA. Translation: AAB81903.1.
AE005176 Genomic DNA. Translation: AAK05306.1. Frameshift.
PIRD45734.
H86775.
RefSeqNP_267364.1. NC_002662.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7MX-ray2.90E/F/G/H1-208[»]
1Z7NX-ray3.25E/F/G/H1-208[»]
ProteinModelPortalQ02129.
SMRQ02129. Positions 1-205.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1114855.
GenomeReviewsGene locus LL1208 in contig AE005176_GR.
KEGGlla:L0066.
PATRIC22294790. VBILacLac136773_1303.

Phylogenomic databases

HOGENOMHBG391868.
ProtClustDBPRK01686.

Enzyme and pathway databases

BioCycLLAC272623:L0066-MONOMER.

Family and domain databases

HAMAPMF_01018. HisG_Short.
[Tree]
InterProIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR024893. ATP_PRibTrfase_HisG_short.
[Graphical view]
KOK00765.
PANTHERPTHR21403. ATP_phspho_trans. 1 hit.
PfamPF01634. HisG. 1 hit.
[Graphical view]
TIGRFAMsTIGR00070. HisG. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS1_LACLA
AccessionPrimary (citable) accession number: Q02129
Secondary accession number(s): Q9CG94
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 26, 2001
Last modified: January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families