Reviewed,
UniProtKB/Swiss-Prot Q9ZMX5 (THRC_HELPJ)
Last modified
July 13, 2010.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and originHide
| Protein names | Recommended name: Threonine synthase Short name=TS EC=4.2.3.1 | ||||
| Gene names |
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| Organism | Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 85963 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributesHide
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)Hide
| Function | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine By similarity. |
| Catalytic activity | O-phospho-L-homoserine + H2O = L-threonine + phosphate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5. |
| Sequence similarities | Belongs to the threonine synthase family. |
OntologiesHide
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Threonine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
SequencesHide
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ReferencesHide
| [1] | "Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. Trust T.J.Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-referencesHide
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001439 Genomic DNA. Translation: AAD05671.1. |
| PIR | A71975. |
| RefSeq | NP_222811.1. |
3D structure databases | |
| SMR | Q9ZMX5. Positions 1-483. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9ZMX5. |
Genome annotation databases | |
| GeneID | 889337. |
| GenomeReviews | Gene locus jhp_0090 in contig AE001439_GR. |
| KEGG | hpj:jhp0090. |
| NMPDR | fig|85963.1.peg.89. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0498. |
| HOGENOM | HBG521025. |
| OMA | FGRIAFQ. |
| ProtClustDB | PRK09225. |
Enzyme and pathway databases | |
| BioCyc | HPYL85963:JHP0090-MONOMER. |
| BRENDA | 4.2.3.1. 295085. |
Family and domain databases | |
| InterPro | IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR004450. Thr_synthase. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR00260. thrC. 1 hit. |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry informationHide
| Entry name | THRC_HELPJ | ||||||||
| Accession | Primary (citable) accession number: Q9ZMX5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documentsHide
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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