UniProtKB - P24670 (AROD_SALTI)
Protein
3-dehydroquinate dehydratase
Gene
aroD
Organism
Salmonella typhi
Status
Functioni
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of Lys-170 at the active site.UniRule annotation1 Publication
Catalytic activityi
- EC:4.2.1.10UniRule annotation1 Publication
Activity regulationi
Inhibited by (2R)-2-methyl-3-dehydroquinic acid.1 Publication
Kineticsi
Kcat is 1.1 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius).1 Publication
- KM=24 µM for 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius)1 Publication
: chorismate biosynthesis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotationProteins known to be involved in the 7 steps of the subpathway in this organism are:
- Phospho-2-dehydro-3-deoxyheptonate aldolase (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG)
- 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
- 3-dehydroquinate dehydratase (aroD), 3-dehydroquinate dehydratase (aroD), 3-dehydroquinate dehydratase (aroD)
- Shikimate dehydrogenase (NADP(+)) (aroE), Shikimate dehydrogenase (NADP(+)) (aroE), Shikimate dehydrogenase (NADP(+)) (aroE)
- Shikimate kinase 2 (aroL), Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK), Shikimate kinase 1 (aroK)
- 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
- Chorismate synthase (aroC), Chorismate synthase (aroC), Chorismate synthase (aroC), Chorismate synthase (aroC)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 21 | 3-dehydroquinateUniRule annotation2 Publications | 1 | |
Binding sitei | 82 | 3-dehydroquinateUniRule annotation1 Publication | 1 | |
Active sitei | 143 | Proton donor/acceptorUniRule annotation1 Publication | 1 | |
Active sitei | 170 | Schiff-base intermediate with substrateUniRule annotation2 Publications | 1 | |
Binding sitei | 213 | 3-dehydroquinateUniRule annotation3 Publications | 1 | |
Binding sitei | 232 | 3-dehydroquinateUniRule annotation2 Publications | 1 | |
Binding sitei | 236 | 3-dehydroquinateUniRule annotation3 Publications | 1 |
GO - Molecular functioni
- 3-dehydroquinate dehydratase activity Source: UniProtKB
GO - Biological processi
- 3,4-dihydroxybenzoate biosynthetic process Source: UniProtKB
- aromatic amino acid family biosynthetic process Source: UniProtKB-UniRule
- chorismate biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Lyase |
Biological process | Amino-acid biosynthesis, Aromatic amino acid biosynthesis |
Ligand | Schiff base |
Enzyme and pathway databases
SABIO-RKi | P24670 |
UniPathwayi | UPA00053;UER00086 |
Names & Taxonomyi
Protein namesi | Recommended name: 3-dehydroquinate dehydratase1 PublicationUniRule annotation (EC:4.2.1.10UniRule annotation1 Publication)Short name: 3-dehydroquinase1 PublicationUniRule annotation Alternative name(s): Type I DHQaseUniRule annotation Type I dehydroquinase1 PublicationUniRule annotation Short name: DHQ11 PublicationUniRule annotation |
Gene namesi | Name:aroD1 PublicationUniRule annotation Ordered Locus Names:STY1760, t1231 |
Organismi | Salmonella typhi |
Taxonomic identifieri | 90370 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella › |
Proteomesi |
|
Pathology & Biotechi
Chemistry databases
DrugBanki | DB03746, 3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000138805 | 1 – 252 | 3-dehydroquinate dehydrataseAdd BLAST | 252 |
Interactioni
Subunit structurei
Dimer of dimers.
UniRule annotation3 PublicationsProtein-protein interaction databases
STRINGi | 220341.16502840 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
PCDDBi | P24670 |
SMRi | P24670 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P24670 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 46 – 48 | 3-dehydroquinate bindingUniRule annotation3 Publications | 3 |
Sequence similaritiesi
Belongs to the type-I 3-dehydroquinase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0710, Bacteria |
HOGENOMi | CLU_064444_0_0_6 |
Family and domain databases
CDDi | cd00502, DHQase_I, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00214, AroD, 1 hit |
InterProi | View protein in InterPro IPR018508, 3-dehydroquinate_DH_AS IPR013785, Aldolase_TIM IPR001381, DHquinase_I |
Pfami | View protein in Pfam PF01487, DHquinase_I, 1 hit |
TIGRFAMsi | TIGR01093, aroD, 1 hit |
PROSITEi | View protein in PROSITE PS01028, DEHYDROQUINASE_I, 1 hit |
i Sequence
Sequence statusi: Complete.
P24670-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKTVTVKNLI IGEGMPKIIV SLMGRDINSV KAEALAYREA TFDILEWRVD
60 70 80 90 100
HFMDIASTQS VLTAARVIRD AMPDIPLLFT FRSAKEGGEQ TITTQHYLTL
110 120 130 140 150
NRAAIDSGLV DMIDLELFTG DADVKATVDY AHAHNVYVVM SNHDFHQTPS
160 170 180 190 200
AEEMVLRLRK MQALGADIPK IAVMPQSKHD VLTLLTATLE MQQHYADRPV
210 220 230 240 250
ITMSMAKEGV ISRLAGEVFG SAATFGAVKQ ASAPGQIAVN DLRSVLMILH
NA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 156 | L → S in CAA38418 (PubMed:2045778).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X54546 Genomic DNA Translation: CAA38418.1 AL513382 Genomic DNA Translation: CAD02002.1 AE014613 Genomic DNA Translation: AAO68886.1 |
PIRi | S15652 |
RefSeqi | NP_456161.1, NC_003198.1 WP_000860215.1, NZ_WSUR01000011.1 |
Genome annotation databases
EnsemblBacteriai | AAO68886; AAO68886; t1231 CAD02002; CAD02002; CAD02002 |
KEGGi | stt:t1231 sty:STY1760 |
PATRICi | fig|220341.7.peg.1771 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X54546 Genomic DNA Translation: CAA38418.1 AL513382 Genomic DNA Translation: CAD02002.1 AE014613 Genomic DNA Translation: AAO68886.1 |
PIRi | S15652 |
RefSeqi | NP_456161.1, NC_003198.1 WP_000860215.1, NZ_WSUR01000011.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1GQN | X-ray | 1.78 | A | 1-252 | [»] | |
1L9W | X-ray | 2.10 | A/B/C/D | 1-252 | [»] | |
1QFE | X-ray | 2.10 | A/B | 1-252 | [»] | |
4CLM | X-ray | 1.40 | A/B | 1-252 | [»] | |
4CNN | X-ray | 1.00 | A/B | 1-252 | [»] | |
4CNO | X-ray | 1.50 | A/B/C/D | 1-252 | [»] | |
4CNP | X-ray | 1.15 | A/B | 1-252 | [»] | |
4UIO | X-ray | 1.35 | A | 1-252 | [»] | |
6H5C | X-ray | 1.14 | A/B | 1-252 | [»] | |
6H5D | X-ray | 1.25 | A/B | 1-252 | [»] | |
6H5G | X-ray | 1.04 | A | 1-252 | [»] | |
6H5J | X-ray | 1.40 | A | 1-252 | [»] | |
6SFE | X-ray | 1.08 | A/B | 1-252 | [»] | |
6SFG | X-ray | 1.23 | A | 1-252 | [»] | |
PCDDBi | P24670 | |||||
SMRi | P24670 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 220341.16502840 |
Chemistry databases
DrugBanki | DB03746, 3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate |
Genome annotation databases
EnsemblBacteriai | AAO68886; AAO68886; t1231 CAD02002; CAD02002; CAD02002 |
KEGGi | stt:t1231 sty:STY1760 |
PATRICi | fig|220341.7.peg.1771 |
Phylogenomic databases
eggNOGi | COG0710, Bacteria |
HOGENOMi | CLU_064444_0_0_6 |
Enzyme and pathway databases
UniPathwayi | UPA00053;UER00086 |
SABIO-RKi | P24670 |
Miscellaneous databases
EvolutionaryTracei | P24670 |
Family and domain databases
CDDi | cd00502, DHQase_I, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00214, AroD, 1 hit |
InterProi | View protein in InterPro IPR018508, 3-dehydroquinate_DH_AS IPR013785, Aldolase_TIM IPR001381, DHquinase_I |
Pfami | View protein in Pfam PF01487, DHquinase_I, 1 hit |
TIGRFAMsi | TIGR01093, aroD, 1 hit |
PROSITEi | View protein in PROSITE PS01028, DEHYDROQUINASE_I, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AROD_SALTI | |
Accessioni | P24670Primary (citable) accession number: P24670 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 1992 |
Last sequence update: | December 5, 2001 | |
Last modified: | December 2, 2020 | |
This is version 152 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- 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