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P58687

- AROD_SALTY

UniProt

P58687 - AROD_SALTY

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Protein
3-dehydroquinate dehydratase
Gene
aroD, STM1358
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Substrate
Active sitei143 – 1431Proton donor/acceptor3 Publications
Active sitei170 – 1701Schiff-base intermediate with substrate3 Publications
Binding sitei213 – 2131Substrate
Binding sitei232 – 2321Substrate
Binding sitei236 – 2361Substrate

GO - Molecular functioni

  1. 3-dehydroquinate dehydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  2. chorismate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1368-MONOMER.
UniPathwayiUPA00053; UER00086.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate dehydratase (EC:4.2.1.10)
Short name:
3-dehydroquinase
Alternative name(s):
Type I DHQase
Gene namesi
Name:aroD
Ordered Locus Names:STM1358
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701K → M: Abolishes enzyme activity. 1 Publication
Mutagenesisi232 – 2321S → A: Reduces enzyme activity 50-fold. 1 Publication
Mutagenesisi236 – 2361Q → A: Nearly abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2522523-dehydroquinate dehydrataseUniRule annotation
PRO_0000138806Add
BLAST

Proteomic databases

PRIDEiP58687.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi99287.STM1358.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Beta strandi9 – 113
Beta strandi13 – 153
Beta strandi17 – 226
Helixi27 – 3711
Beta strandi43 – 486
Helixi49 – 513
Turni53 – 564
Helixi58 – 7114
Beta strandi77 – 804
Helixi84 – 863
Helixi94 – 10714
Beta strandi111 – 1166
Helixi117 – 1193
Helixi121 – 13313
Beta strandi137 – 14610
Helixi151 – 16313
Beta strandi167 – 1737
Helixi178 – 19417
Beta strandi201 – 2044
Helixi207 – 2104
Helixi211 – 2144
Helixi216 – 2194
Beta strandi223 – 2253
Beta strandi227 – 2293
Helixi239 – 25113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L2IX-ray1.85A/B1-252[»]
3LB0X-ray1.65A/B1-252[»]
3M7WX-ray1.95A/B/C/D/E/F1-252[»]
3NNTX-ray1.60A/B1-252[»]
3O1NX-ray1.03A/B1-252[»]
3OEXX-ray1.90A/B/C/D1-252[»]
3S42X-ray1.45A/B1-252[»]
4GFSX-ray1.80A/B1-252[»]
4GUFX-ray1.50A/B1-252[»]
4GUGX-ray1.62A/B1-252[»]
4GUHX-ray1.95A/B1-252[»]
4GUIX-ray1.78A/B1-252[»]
4GUJX-ray1.50A/B1-252[»]
4IUOX-ray1.80A/B1-252[»]
ProteinModelPortaliP58687.
SMRiP58687. Positions 1-252.

Miscellaneous databases

EvolutionaryTraceiP58687.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 483Substrate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000105514.
KOiK03785.
OMAiEGMPKII.
OrthoDBiEOG6P33BK.
PhylomeDBiP58687.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00214. AroD.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]
PfamiPF01487. DHquinase_I. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01093. aroD. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P58687-1 [UniParc]FASTAAdd to Basket

« Hide

MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD    50
HFANVTTAES VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL 100
NRAAVDSGLV DMIDLELFTG DDEVKATVGY AHQHNVAVIM SNHDFHKTPA 150
AEEIVQRLRK MQELGADIPK IAVMPQTKAD VLTLLTATVE MQERYADRPI 200
ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA DLRTVLTILH 250
QA 252
Length:252
Mass (Da):27,325
Last modified:January 31, 2002 - v1
Checksum:i10BB561E38EA0A75
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL20283.1.
RefSeqiNP_460324.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20283; AAL20283; STM1358.
GeneIDi1252876.
KEGGistm:STM1358.
PATRICi32381199. VBISalEnt20916_1442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL20283.1 .
RefSeqi NP_460324.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L2I X-ray 1.85 A/B 1-252 [» ]
3LB0 X-ray 1.65 A/B 1-252 [» ]
3M7W X-ray 1.95 A/B/C/D/E/F 1-252 [» ]
3NNT X-ray 1.60 A/B 1-252 [» ]
3O1N X-ray 1.03 A/B 1-252 [» ]
3OEX X-ray 1.90 A/B/C/D 1-252 [» ]
3S42 X-ray 1.45 A/B 1-252 [» ]
4GFS X-ray 1.80 A/B 1-252 [» ]
4GUF X-ray 1.50 A/B 1-252 [» ]
4GUG X-ray 1.62 A/B 1-252 [» ]
4GUH X-ray 1.95 A/B 1-252 [» ]
4GUI X-ray 1.78 A/B 1-252 [» ]
4GUJ X-ray 1.50 A/B 1-252 [» ]
4IUO X-ray 1.80 A/B 1-252 [» ]
ProteinModelPortali P58687.
SMRi P58687. Positions 1-252.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM1358.

Proteomic databases

PRIDEi P58687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20283 ; AAL20283 ; STM1358 .
GeneIDi 1252876.
KEGGi stm:STM1358.
PATRICi 32381199. VBISalEnt20916_1442.

Phylogenomic databases

HOGENOMi HOG000105514.
KOi K03785.
OMAi EGMPKII.
OrthoDBi EOG6P33BK.
PhylomeDBi P58687.

Enzyme and pathway databases

UniPathwayi UPA00053 ; UER00086 .
BioCyci SENT99287:GCTI-1368-MONOMER.

Miscellaneous databases

EvolutionaryTracei P58687.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00214. AroD.
InterProi IPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view ]
Pfami PF01487. DHquinase_I. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01093. aroD. 1 hit.
PROSITEi PS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  2. "New insights into the mechanism of the Schiff base hydrolysis catalyzed by type I dehydroquinate dehydratase from S. enterica: a theoretical study."
    Yao Y., Li Z.S.
    Org. Biomol. Chem. 10:7037-7044(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  3. "A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding."
    Light S.H., Minasov G., Shuvalova L., Peterson S.N., Caffrey M., Anderson W.F., Lavie A.
    Biochemistry 50:2357-2363(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF SER-232 AND GLN-236.
  4. "Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates."
    Light S.H., Minasov G., Shuvalova L., Duban M.E., Caffrey M., Anderson W.F., Lavie A.
    J. Biol. Chem. 286:3531-3539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-170 IN COMPLEX WITH 3-DEHYDROQUINIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF LYS-170.

Entry informationi

Entry nameiAROD_SALTY
AccessioniPrimary (citable) accession number: P58687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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