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Q95WL3

- Q95WL3_TRYCR

UniProt

Q95WL3 - Q95WL3_TRYCR

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Protein
Submitted name:

Farnesyl pyrophosphate synthase

Gene
N/A
Organism
Trypanosoma cruzi
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761SodiumImported
Metal bindingi190 – 1901SodiumImported
Metal bindingi191 – 1911Sodium; via amide nitrogenImported

GO - Molecular functioni

  1. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. isoprenoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Biological processi

Isoprene biosynthesisUniRule annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Farnesyl pyrophosphate synthaseImported
OrganismiTrypanosoma cruziImported
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IBAX-ray2.40A1-362[»]
3ICKX-ray2.40A1-362[»]
3ICMX-ray2.20A1-362[»]
3ICNX-ray2.40A1-362[»]
3ICZX-ray2.15A1-362[»]
4DWBX-ray2.10A1-362[»]
4DWGX-ray2.01A1-362[»]
4DXJX-ray2.35A/B/C1-362[»]
4DZWX-ray3.05A1-362[»]
4E1EX-ray2.65A2-362[»]
ProteinModelPortaliQ95WL3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.UniRule annotation

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q95WL3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASMERFLSV YDEVQAFLLD QLQSKYEIDP NRARYLRIMM DTTCLGGKYF
60 70 80 90 100
RGMTVVNVAE GFLAVTQHDE ATKERILHDA CVGGWMIEFL QAHYLVEDDI
110 120 130 140 150
MDGSVMRRGK PCWYRFPGVT TQCAINDGII LKSWTQIMAW HYFADRPFLK
160 170 180 190 200
DLLCLFQKVD YATAVGQMYD VTSMCDSNKL DPEVAQPMTT DFAEFTPAIY
210 220 230 240 250
KRIVKYKTTF YTYLLPLVMG LFVSEAAASV EMNLVERVAH LIGEYFQVQD
260 270 280 290 300
DVMDCFTPPE QLGKVGTDIE DAKCSWLAVT FLGKANAAQV AEFKANYGDK
310 320 330 340 350
DPAKVAVVKR LYSEANLQAD FAAYEAEVVR EVESLIEQLK VKSPTFAESV
360
AVVWEKTHKR KK
Length:362
Mass (Da):41,180
Last modified:December 1, 2001 - v1
Checksum:iCF2CB54BA03B3DB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei362 – 3621Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312690 Genomic DNA. Translation: AAK71861.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312690 Genomic DNA. Translation: AAK71861.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IBA X-ray 2.40 A 1-362 [» ]
3ICK X-ray 2.40 A 1-362 [» ]
3ICM X-ray 2.20 A 1-362 [» ]
3ICN X-ray 2.40 A 1-362 [» ]
3ICZ X-ray 2.15 A 1-362 [» ]
4DWB X-ray 2.10 A 1-362 [» ]
4DWG X-ray 2.01 A 1-362 [» ]
4DXJ X-ray 2.35 A/B/C 1-362 [» ]
4DZW X-ray 3.05 A 1-362 [» ]
4E1E X-ray 2.65 A 2-362 [» ]
ProteinModelPortali Q95WL3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF00348. polyprenyl_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Bisphosphonates are potent inhibitors of Trypanosoma cruzi farnesyl pyrophosphate synthase."
    Montalvetti A., Bailey B.N., Martin M.B., Severin G.W., Oldfield E., Docampo R.
    J. Biol. Chem. 276:33930-33937(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma cruzi farnesyl diphosphate synthase homodimer."
    Huang C.H., Gabelli S.B., Oldfield E., Amzel L.M.
    Proteins 78:888-899(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  3. "Design, synthesis, calorimetry, and crystallographic analysis of 2-alkylaminoethyl-1,1-bisphosphonates as inhibitors of Trypanosoma cruzi farnesyl diphosphate synthase."
    Aripirala S., Szajnman S.H., Jakoncic J., Rodriguez J.B., Docampo R., Gabelli S.B., Amzel L.M.
    J. Med. Chem. 55:6445-6454(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).

Entry informationi

Entry nameiQ95WL3_TRYCR
AccessioniPrimary (citable) accession number: Q95WL3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3