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P58687

- AROD_SALTY

UniProt

P58687 - AROD_SALTY

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Protein

3-dehydroquinate dehydratase

Gene

aroD

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 PublicationsUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Substrate
Active sitei143 – 1431Proton donor/acceptor
Active sitei170 – 1701Schiff-base intermediate with substrate
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 dehydrataseUniRule annotation (EC:4.2.1.10UniRule annotation)
Short name:
3-dehydroquinaseUniRule annotation
Alternative name(s):
Type I DHQaseUniRule annotation
Gene namesi
Name:aroDUniRule annotation
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 dehydratasePRO_0000138806Add
BLAST

Proteomic databases

PRIDEiP58687.

Interactioni

Subunit structurei

Homodimer.2 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi99287.STM1358.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi9 – 113Combined sources
Beta strandi13 – 153Combined sources
Beta strandi17 – 226Combined sources
Helixi27 – 3711Combined sources
Beta strandi43 – 486Combined sources
Helixi49 – 513Combined sources
Turni53 – 564Combined sources
Helixi58 – 7114Combined sources
Beta strandi77 – 804Combined sources
Helixi84 – 863Combined sources
Helixi94 – 10714Combined sources
Beta strandi111 – 1166Combined sources
Helixi117 – 1193Combined sources
Helixi121 – 13313Combined sources
Beta strandi137 – 14610Combined sources
Helixi151 – 16313Combined sources
Beta strandi167 – 1737Combined sources
Helixi178 – 19417Combined sources
Beta strandi201 – 2044Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 2144Combined sources
Helixi216 – 2194Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi227 – 2293Combined sources
Helixi239 – 25113Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58687.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the type-I 3-dehydroquinase family.UniRule annotation

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

        10         20         30         40         50
MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD
60 70 80 90 100
HFANVTTAES VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL
110 120 130 140 150
NRAAVDSGLV DMIDLELFTG DDEVKATVGY AHQHNVAVIM SNHDFHKTPA
160 170 180 190 200
AEEIVQRLRK MQELGADIPK IAVMPQTKAD VLTLLTATVE MQERYADRPI
210 220 230 240 250
ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA DLRTVLTILH

QA
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: October 29, 2014
This is version 91 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