Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Squalene/Phytoene Synthase Like

     ⌊ Family dehydrosqualene synthase

  ⌊ FunctionalDomain dehydrosqualene synthase (ID 132227)

Superfamily Assignment Evidence Code(s) FSM PubMed:18276850
Family Assignment Evidence Code CFM PubMed:18276850
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Staphylococcus aureus Taxon ID: 1280 446100464 WP_000178319.1 (RefSeq) URP
Staphylococcus aureus Taxon ID: 1280 827297287 KLM87604.1 (Genbank) URP
Staphylococcus aureus Taxon ID: 1280 827294316 KLM84634.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
4,4'-diapophytoene synthase {ECO:0000250|UniProtKB:Q2FV59} A9JQL9 CRTM_STAAU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 287 | Length of Functional Domain: 287

1       10        20        30        40        50        60

MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFL
NQIKEDIQSIEKYPYEYHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMF
ETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFENE
RIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFRDVMDQIKVFSIEAQPI
IELAARIYIEILDEVRQANYTLHERVFVEKRKKAKLFHEINSKYHRI
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
48 Asp (D) side chain None --
52 Asp (D) side chain None --
168 Asn (N) side chain None --
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
45 Arg (R) side chain None -- ICS PubMed:21098670
48 Asp (D) side chain Metal ligand metal ligand -- binding ICS
52 Asp (D) side chain Metal ligand metal ligand -- binding ICS
129 Tyr (Y) side chain facilitates removal of Mg2+ PPi product complex formed in both half-reactions increase electrophilicity -- spectator IME PubMed:21098670
168 Asn (N) side chain Metal ligand metal ligand -- binding ICS
172 Asp (D) side chain Metal ligand metal ligand -- binding ICS
176 Asp (D) side chain None -- IME PubMed:21098670
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
45 Arg (R) side chain None -- ICS PubMed:21098670
48 Asp (D) side chain None -- IME PubMed:21098670
52 Asp (D) side chain None -- IME PubMed:21098670
129 Tyr (Y) side chain facilitates removal of Mg2+ PPi product complex formed in both half-reactions increase electrophilicity -- spectator IME PubMed:21098670
172 Asp (D) side chain None -- IME PubMed:21098670
176 Asp (D) side chain None -- IME PubMed:21098670

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2ZCQ Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bisphosphonate Bph-652 Dehydrosqualene Synthase 33 2.38 (1R)-4-(3-Phenoxyphenyl)-1-Phosphonobutane-1-Sulfonic Acid • Magnesium Ion CSA • PDB • PDBSum
2ZCS Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bisphosphonate Bph-700 Dehydrosqualene Synthase 33 2.03 Tripotassium (1R)-4-Biphenyl-4-Yl-1-Phosphonatobutane-1-Sulfonate CSA • PDB • PDBSum
2ZCR Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bisphosphonate Bph-698 Dehydrosqualene Synthase 33 1.92 Tripotassium (1R)-4-(4'-Butylbiphenyl-4-Yl)-1-Phosphonatobutane-1-Sulfonate • Magnesium Ion CSA • PDB • PDBSum
3NRI Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From S. Aureus Complexed With Dehydrosqualene (Dhs) Dehydrosqualene Synthase 33 2.85 (6E,10R,13S,18E)-2,6,10,15,19,23-Hexamethyltetracosa-2, 6,10,11,13,14,18,22-Octaene CSA • PDB • PDBSum
3NPR Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From S. Aureus Complexed With Presqualene Diphosphate (Pspp) Dehydrosqualene Synthase 33 2.0 {(1R,2R,3R)-2-[(3E)-4,8-Dimethylnona-3,7-Dien-1-Yl]-2-Methyl-3-[(1E,5E)-2,6,10-Trimethylundeca-1,5,9-Trien-1-Yl]Cyclopropyl}Methyl Trihydrogen Diphosphate • Magnesium Ion CSA • PDB • PDBSum
3TFP Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Bph-1162 Dehydrosqualene Synthase 33 2.0 Magnesium Ion • 2-({2-Chloro-6-[(2,4-Dichlorophenyl) Sulfanyl]Benzyl}Carbamoyl)Benzoic Acid CSA • PDB • PDBSum
2ZY1 Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bisphosphonate Bph-830 Dehydrosqualene Synthase 33 1.78 Dipotassium (2-Oxo-2-{[3-(3-Phenoxyphenyl) Propyl]Amino}Ethyl)Phosphonate CSA • PDB • PDBSum
3TFV Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Bph-1154 Dehydrosqualene Synthase 33 3.0 Magnesium Ion • 5-Bromo-2-{[3-(Octyloxy)Benzyl]Sulfanyl}Benzoic Acid CSA • PDB • PDBSum
3ACW Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bph-651 Dehydrosqualene Synthase 33 1.63 (3R)-3-Biphenyl-4-Yl-1-Azabicyclo[2.2.2]Octan-3-Ol CSA • PDB • PDBSum
3TFN Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Bph-1183 Dehydrosqualene Synthase 33 2.07 (1-{2-[4-(Diphenylmethyl)Piperazin-1-Yl]-2-Oxoethyl}Cyclopentyl)Acetic Acid • Magnesium Ion CSA • PDB • PDBSum
3ACY Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bph-702 Dehydrosqualene Synthase 33 1.84 (1R)-4-[3-(2-Benzylphenoxy)Phenyl]-1-Phosphonobutane-1-Sulfonic Acid • Magnesium Ion CSA • PDB • PDBSum
3ACX Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Bph-673 Dehydrosqualene Synthase 33 1.31 N-(1-Methylethyl)-3-[(3-Prop-2-En-1-Ylbiphenyl-4-Yl) Oxy]Propan-1-Amine CSA • PDB • PDBSum
2ZCO Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Dehydrosqualene Synthase 33 1.58 CSA • PDB • PDBSum
4E9Z Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Quinuclidine Bph-651 In The S1 Site Dehydrosqualene Synthase 33 2.06 (3R)-3-Biphenyl-4-Yl-1-Azabicyclo[2.2.2]Octan-3-Ol CSA • PDB • PDBSum
4EA2 Crystal Structure Of Dehydrosqualene Synthase (Crtm) Aureus Complexed With Sq-109 Dehydrosqualene Synthase 33 2.05 N-[(2Z)-3,7-Dimethylocta-2,6-Dien-1-Yl]-N'-[(1R,3S,5R, 7R)-Tricyclo[3.3.1.1~3,7~]Dec-2-Yl]Ethane-1,2-Diamine
(2 more ⇓) 		CSA • PDB • PDBSum
4EA0 Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Diphosphate And Quinuclidine Bph-651 Dehydrosqualene Synthase 33 2.12 Magnesium Ion
(3 more ⇓) 		CSA • PDB • PDBSum
4EA1 Co-Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus With Sq-109 Dehydrosqualene Synthase 33 2.46 N-[(2E)-3,7-Dimethylocta-2,6-Dien-1-Yl]-N'-[(1R,3S,5R, 7R)-Tricyclo[3.3.1.1~3,7~]Dec-2-Yl]Ethane-1,2-Diamine CSA • PDB • PDBSum
4E9U Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With A Thiocyanate Inhibitor Dehydrosqualene Synthase 33 2.1 2-(4-Phenoxyphenoxy)Ethyl Thiocyanate • Magnesium Ion CSA • PDB • PDBSum
4F6V Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Bph-1034, Mg2+ And Fmp. Dehydrosqualene Synthase 33 2.3 2,4-Dioxo-4-{[3-(3-Phenoxyphenyl)Propyl]Amino}Butanoic Acid
(3 more ⇓) 		CSA • PDB • PDBSum
4F6X Crystal Structure Of Dehydrosqualene Synthase (Crtm) From S. Aureus Complexed With Bph-1112 Dehydrosqualene Synthase 33 1.98 1-[3-(Hexyloxy)Benzyl]-4-Hydroxy-2-Oxo-1,2-Dihydropyridine-3-Carboxylic Acid
(2 more ⇓) 		CSA • PDB • PDBSum
3W7F Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Farnesyl Thiopyrophosphate Dehydrosqualene Synthase 33 2.25 S-[(2E,6E)-3,7,11-Trimethyldodeca-2,6,10-Trienyl] Trihydrogen Thiodiphosphate • Magnesium Ion CSA • PDB • PDBSum
3VJE Crystal Structure Of The Y248A Mutant Of C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus In Complex With Zaragozic Acid A Dehydrosqualene Synthase 33 2.12 Yes Zaragozic Acid A CSA • PDB • PDBSum
3VJD Crystal Structure Of The Y248A Mutant Of C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Dehydrosqualene Synthase 33 1.48 Yes L(+)-Tartaric Acid CSA • PDB • PDBSum
3ADZ Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Intermediate Pspp Dehydrosqualene Synthase 33 1.89 Yes {(1R,2R,3R)-2-[(3E)-4,8-Dimethylnona-3,7-Dien-1-Yl]-2-Methyl-3-[(1E,5E)-2,6,10-Trimethylundeca-1,5,9-Trien-1-Yl]Cyclopropyl}Methyl Trihydrogen Diphosphate • Magnesium Ion CSA • PDB • PDBSum
3LGZ Crystal Structure Of Dehydrosqualene Synthase Y129A From S. Aureus Complexed With Presqualene Pyrophosphate Dehydrosqualene Synthase 33 2.41 Yes {(1R,2R,3R)-2-[(3E)-4,8-Dimethylnona-3,7-Dien-1-Yl]-2-Methyl-3-[(1E,5E)-2,6,10-Trimethylundeca-1,5,9-Trien-1-Yl]Cyclopropyl}Methyl Trihydrogen Diphosphate • Magnesium Ion CSA • PDB • PDBSum
3AE0 Crystal Structure Of The C(30) Carotenoid Dehydrosqualene Synthase From Staphylococcus Aureus Complexed With Geranylgeranyl Thiopyrophosphate Dehydrosqualene Synthase 33 2.37 Yes Phosphonooxy-[(10E)-3,7,11,15-Tetramethylhexadeca-2,6, 10,14-Tetraenyl]Sulfanyl-Phosphinic Acid • Magnesium Ion CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 11:48 a.m. update curation agent sbrown setDomainBoundaries.py
update domain start position 6 1
EC number assigned by UniProtKB accession ID.