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Protein

3-dehydroquinate synthase

Gene

aroB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • NAD+By similarity
  • Co2+By similarity, Zn2+By similarityNote: Binds 1 divalent metal cation per subunit. Can use either Co2+ or Zn2+.By similarity

Pathwayi: chorismate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (VC_1507), Phospho-2-dehydro-3-deoxyheptonate aldolase (VC_0695)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroQ)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Cobalt, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate synthase (EC:4.2.3.4)
Gene namesi
Name:aroB
Ordered Locus Names:VC_2628
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3613613-dehydroquinate synthasePRO_0000140804Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi243277.VC2628.

Structurei

Secondary structure

361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 66Combined sources
Helixi9 – 113Combined sources
Beta strandi13 – 186Combined sources
Helixi21 – 233Combined sources
Helixi25 – 284Combined sources
Beta strandi35 – 417Combined sources
Turni42 – 443Combined sources
Helixi45 – 5915Combined sources
Beta strandi62 – 687Combined sources
Helixi72 – 743Combined sources
Helixi77 – 8913Combined sources
Beta strandi97 – 1037Combined sources
Helixi104 – 11613Combined sources
Beta strandi122 – 1276Combined sources
Helixi130 – 1356Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi160 – 1656Combined sources
Helixi166 – 1716Combined sources
Helixi174 – 19017Combined sources
Helixi193 – 20715Combined sources
Helixi211 – 23323Combined sources
Helixi238 – 2436Combined sources
Helixi246 – 25611Combined sources
Turni258 – 2603Combined sources
Helixi263 – 28018Combined sources
Helixi286 – 29813Combined sources
Helixi311 – 3188Combined sources
Helixi320 – 3223Combined sources
Beta strandi330 – 3367Combined sources
Beta strandi339 – 3446Combined sources
Helixi348 – 35710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OKFX-ray2.50A/B1-361[»]
ProteinModelPortaliQ9KNV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dehydroquinate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105D49. Bacteria.
COG0337. LUCA.
KOiK01735.
OMAiIERSCAA.
OrthoDBiEOG6SJJGD.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.
TIGRFAMsiTIGR01357. aroB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9KNV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERITVNLGE RSYPISIGAG LFANPALLSL SAKQKVVIVT NHTVAPLYAP
60 70 80 90 100
AIISLLDHIG CQHALLELPD GEQYKTLETF NTVMSFLLEH NYSRDVVVIA
110 120 130 140 150
LGGGVIGDLV GFAAACYQRG VDFIQIPTTL LSQVDSSVGG KTAVNHPLGK
160 170 180 190 200
NMIGAFYQPK AVVIDTDCLT TLPAREFAAG MAEVIKYGII YDSAFFDWLE
210 220 230 240 250
AQMEALYALD EQALTYAIAR CCQIKAEVVA QDEKESGIRA LLNLGHTFGH
260 270 280 290 300
AIEAHMGYGN WLHGEAVSAG TVMAAKTAQL QGLIDASQFE RILAILKKAH
310 320 330 340 350
LPVRTPENMT FADFMQHMMR DKKVLAGELR LVLPTSIGTS AVVKGVPEAV
360
IAQAIEYCRT V
Length:361
Mass (Da):39,049
Last modified:August 13, 2002 - v2
Checksum:iD0388B733EFD3F2A
GO

Sequence cautioni

The sequence AAF95769.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95769.1. Different initiation.
PIRiB82053.
RefSeqiNP_232256.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95769; AAF95769; VC_2628.
GeneIDi2615645.
KEGGivch:VC2628.
PATRICi20084280. VBIVibCho83274_2506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95769.1. Different initiation.
PIRiB82053.
RefSeqiNP_232256.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OKFX-ray2.50A/B1-361[»]
ProteinModelPortaliQ9KNV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC2628.

Protocols and materials databases

DNASUi2615645.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95769; AAF95769; VC_2628.
GeneIDi2615645.
KEGGivch:VC2628.
PATRICi20084280. VBIVibCho83274_2506.

Phylogenomic databases

eggNOGiENOG4105D49. Bacteria.
COG0337. LUCA.
KOiK01735.
OMAiIERSCAA.
OrthoDBiEOG6SJJGD.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.
TIGRFAMsiTIGR01357. aroB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiAROB_VIBCH
AccessioniPrimary (citable) accession number: Q9KNV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: August 13, 2002
Last modified: March 16, 2016
This is version 96 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.