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Protein

Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific)

Gene

Tfu_0853

Organism
Thermobifida fusca (strain YX)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of Z,E-mixed prenyl diphosphates by a condensation of isopentenyl diphosphate to an allylic diphosphate. It shows a large substrate specificity accepting dimethylallyl diphosphate (DMAPP), GPP, E,Efarnesyl diphosphate (FPP), E,E,E-geranylgeranyl diphosphate (GGPP), neryl diphosphate (Z-GPP), and (2Z,6E)-farnesyl diphosphate (Z,E-FPP) as allylic substrates. The enzyme exhibits the highest activity when Z,E-FPP is employed as an allylic substrate. The major product is dodecaprenyl diphosphate (C60) under every allylic substrate conditions, but the enzyme is also able to synthesize even C70 prenyl diphosphate as the maximum chain-length product.1 Publication

Catalytic activityi

(2Z,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + trans,polycis-polyprenyl diphosphate (n = 9-11).1 Publication

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441By similarity
Metal bindingi44 – 441MagnesiumBy similarity
Binding sitei49 – 491SubstrateBy similarity
Binding sitei57 – 571SubstrateBy similarity
Binding sitei61 – 611SubstrateBy similarity
Active sitei92 – 921Proton acceptorBy similarity
Binding sitei93 – 931SubstrateBy similarity
Binding sitei95 – 951SubstrateBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Metal bindingi231 – 2311MagnesiumBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB-HAMAP
  • prenyltransferase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15682.
TFUS269800:GI42-869-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific) (EC:2.5.1.88)
Alternative name(s):
Cis-prenyltransferase
Dodecaprenyl diphosphate synthase
Gene namesi
Ordered Locus Names:Tfu_0853
OrganismiThermobifida fusca (strain YX)
Taxonomic identifieri269800 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida
Proteomesi
  • UP000000434 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific)PRO_0000419134Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi269800.Tfu_0853.

Structurei

3D structure databases

ProteinModelPortaliQ47RM6.
SMRiQ47RM6. Positions 15-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingBy similarity
Regioni89 – 913Substrate bindingBy similarity
Regioni218 – 2203Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
HOGENOMiHOG000006055.
KOiK00806.
OMAiWNRPKLE.
OrthoDBiEOG68H89T.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47RM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPKTVFSTD THREPIPPQP HPSGARPPQL PRELIPRHVA IVMDGNGRWA
60 70 80 90 100
KQRGLPRTEG HKAGESSLFD VIEGALELGV PYLSAYAFST ENWKRSPDEV
110 120 130 140 150
RFLMGFNRDV IRRRRDELHA RGVRVRWAGR PGRLWKSVIK ELTEAEELTK
160 170 180 190 200
HNTKLTLQFC VNYGGRAEIA DAAAALARDV AAGRLSPNRV TEATLARYLY
210 220 230 240 250
HPDIPDVDLF IRSSGEQRLS NFLLWQSSYA EFVFLDTLWP DFDRRHFWQA
260 270 280
CEIYARRDRR YGGAEPNPVG PPQSAAGAQG QD
Length:282
Mass (Da):31,967
Last modified:September 13, 2005 - v1
Checksum:iA1085BD7CB076E90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000088 Genomic DNA. Translation: AAZ54891.1.
RefSeqiWP_011291300.1. NC_007333.1.

Genome annotation databases

EnsemblBacteriaiAAZ54891; AAZ54891; Tfu_0853.
KEGGitfu:Tfu_0853.
PATRICi23902172. VBITheFus33945_0888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000088 Genomic DNA. Translation: AAZ54891.1.
RefSeqiWP_011291300.1. NC_007333.1.

3D structure databases

ProteinModelPortaliQ47RM6.
SMRiQ47RM6. Positions 15-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_0853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ54891; AAZ54891; Tfu_0853.
KEGGitfu:Tfu_0853.
PATRICi23902172. VBITheFus33945_0888.

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
HOGENOMiHOG000006055.
KOiK00806.
OMAiWNRPKLE.
OrthoDBiEOG68H89T.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15682.
TFUS269800:GI42-869-MONOMER.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YX.
  2. "Cloning and functional analysis of cis-prenyltransferase from Thermobifida fusca."
    Ambo T., Noike M., Kurokawa H., Koyama T.
    J. Biosci. Bioeng. 107:620-622(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DODECAPRENYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiDPDP_THEFY
AccessioniPrimary (citable) accession number: Q47RM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 13, 2005
Last modified: November 11, 2015
This is version 71 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

Complete proteome, Reference proteome

Documents

  1. 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.