Q02129 (HIS1_LACLA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 92.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: ATP phosphoribosyltransferase Short name=ATP-PRT Short name=ATP-PRTase EC=2.4.2.17 | ||||||
| Gene names |
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| Organism | Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) | ||||||
| Taxonomic identifier | 272623 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus |
Protein attributes
| Sequence length | 208 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP phosphoribosyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 208 | 208 | ATP phosphoribosyltransferase HAMAP MF_01018 | PRO_0000151911 | ||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 51 | 1 | P → A in AAB81903. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 86 | 1 | Y → D in AAB81903. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 110 | 1 | H → R in AAB81903. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 7 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 10 – 20 | 11 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 21 – 23 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 36 – 38 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 46 – 49 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 51 – 59 | 9 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 64 – 69 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 70 – 75 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 87 | 7 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 93 – 98 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 100 – 104 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 116 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 118 – 127 | 10 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 132 – 136 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 143 – 146 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 160 | 10 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 164 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 165 – 167 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 169 – 176 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 179 – 184 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 202 | 18 | ||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. | ||||||||||||||||||
| PIR | D45734. H86775. | ||||||||||||||||||
| RefSeq | NP_267364.1. NC_002662.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q02129. | ||||||||||||||||||
| SMR | Q02129. Positions 1-205. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 1114855. | ||||||||||||||||||
| GenomeReviews | Gene locus LL1208 in contig AE005176_GR. | ||||||||||||||||||
| KEGG | lla:L0066. | ||||||||||||||||||
| PATRIC | 22294790. VBILacLac136773_1303. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | HBG391868. | ||||||||||||||||||
| ProtClustDB | PRK01686. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | LLAC272623:L0066-MONOMER. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_01018. HisG_Short. [Tree] | ||||||||||||||||||
| InterPro | IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. IPR001348. ATP_PRibTrfase_HisG. IPR024893. ATP_PRibTrfase_HisG_short. [Graphical view] | ||||||||||||||||||
| KO | K00765. | ||||||||||||||||||
| PANTHER | PTHR21403. ATP_phspho_trans. 1 hit. | ||||||||||||||||||
| Pfam | PF01634. HisG. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR00070. HisG. 1 hit. | ||||||||||||||||||
| PROSITE | PS01316. ATP_P_PHORIBOSYLTR. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | HIS1_LACLA | ||||||||
| Accession | Primary (citable) accession number: Q02129 Secondary accession number(s): Q9CG94 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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 |

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