Q8FV25 (DAPD_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
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: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase EC=2.3.1.117 Alternative name(s): Tetrahydrodipicolinate N-succinyltransferase Short name=THDP succinyltransferase Short name=THP succinyltransferase Short name=Tetrahydropicolinate succinylase | ||||
| Gene names |
| ||||
| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 284 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. HAMAP-Rule MF_00811 |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. HAMAP-Rule MF_00811 |
| Subunit structure | Homotrimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the transferase hexapeptide repeat family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Molecular function | Acyltransferase Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via diaminopimelateInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 284 | 284 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase HAMAP-Rule MF_00811 | PRO_0000196922 | |||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 111 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 148 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 7 – 18 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 19 – 22 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 29 – 43 | 15 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 52 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 58 – 60 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 74 | 13 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 81 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 84 – 86 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 92 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 96 – 99 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 102 – 108 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 119 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 132 – 135 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 153 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 221 – 223 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 224 – 226 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 232 – 234 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 238 – 246 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 258 – 267 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 270 – 275 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 278 – 283 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [3] | "Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate n-succinyltransferase from Brucella melitensis biovar abortus 2308." Seattle structural genomics center for infectious disease (SSGCID) Submitted (SEP-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE014292 Genomic DNA. Translation: AAN34196.1. CP002998 Genomic DNA. Translation: AEM20472.1. | ||||||||||||
| PIR | AD3543. | ||||||||||||
| RefSeq | NP_700191.1. NC_004311.2. YP_005614698.1. NC_017250.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q8FV25. | ||||||||||||
| SMR | Q8FV25. Positions 6-283. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 204722.BRA1028. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q8FV25. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAN34196; AAN34196; BRA1028. AEM20472; AEM20472; BS1330_II1020. | ||||||||||||
| GeneID | 1165473. 12139253. | ||||||||||||
| KEGG | bms:BRA1028. bsi:BS1330_II1020. | ||||||||||||
| PATRIC | 17794891. VBIBruSui107850_3253. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG2171. | ||||||||||||
| HOGENOM | HOG000003295. | ||||||||||||
| KO | K00674. | ||||||||||||
| OMA | NQWAKKA. | ||||||||||||
| ProtClustDB | PRK11830. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| UniPathway | UPA00034; UER00019. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.166.10. 1 hit. | ||||||||||||
| HAMAP | MF_00811. DapD. | ||||||||||||
| InterPro | IPR005664. DapD_Trfase_Hexpep_rpt_fam. IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR023180. THP_succinylTrfase_dom1. IPR011004. Trimer_LpxA-like. [Graphical view] | ||||||||||||
| PANTHER | PTHR19136:SF52. PTHR19136:SF52. 1 hit. | ||||||||||||
| Pfam | PF00132. Hexapep. 2 hits. [Graphical view] | ||||||||||||
| SUPFAM | SSF51161. Trimer_LpxA_like. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00965. dapD. 1 hit. | ||||||||||||
| PROSITE | PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q8FV25. | ||||||||||||
Entry information
| Entry name | DAPD_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FV25 Secondary accession number(s): G0KE34 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| 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 |

Clusters with
