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P53610 (PGTB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Geranylgeranyl transferase type-1 subunit beta
EC=2.5.1.59
Alternative name(s):
Geranylgeranyl transferase type I subunit beta
Short name=GGTase-I-beta
Type I protein geranyl-geranyltransferase subunit beta
Gene names
Name:Pggt1b
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Acts on the Rac1, Rac2, Rap1A and Rap1B proteins. The beta subunit is responsible for peptide-binding.

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Heterodimer of an alpha and a beta subunit. Ref.2

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 4 PFTB repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FntaQ046315EBI-602610,EBI-602447

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Geranylgeranyl transferase type-1 subunit beta
PRO_0000119771

Regions

Repeat144 – 18643PFTB 1
Repeat193 – 23442PFTB 2
Repeat245 – 28440PFTB 3
Repeat291 – 33343PFTB 4

Sites

Metal binding2691Zinc
Metal binding2711Zinc
Metal binding3211Zinc

Secondary structure

1 ................................................ 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53610 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: AADEC7301A4A4011

FASTA37742,414
        10         20         30         40         50         60 
MAATEDDRLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM 

        70         80         90        100        110        120 
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL DRCGFRGSSY LGIPFNPSKN PGTAHPYDSG 

       130        140        150        160        170        180 
HIAMTYTGLS CLIILGDDLS RVDKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC 

       190        200        210        220        230        240 
ICYMLNNWSG MDMKKAISYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF 

       250        260        270        280        290        300 
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS 

       310        320        330        340        350        360 
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLRDLHQS 

       370 
WKTKDSKQCS DNVHISS

« Hide

References

[1]"cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I."
Zhang F.L., Diehl R.E., Kohl N.E., Gibbs J.B., Giros B., Casey P.J., Omer C.A.
J. Biol. Chem. 269:3175-3180(1994) [PubMed: 8106351] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Structure of mammalian protein geranylgeranyltransferase type-I."
Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
EMBO J. 22:5963-5974(2003) [PubMed: 14609943] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L24116 mRNA. Translation: AAA17756.1.
IPIIPI00211844.
PIRB53044.
RefSeqNP_112344.1. NM_031082.1.
UniGeneRn.10031.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4PX-ray2.65B/D/F/H/J/L1-377[»]
1N4QX-ray2.40B/D/F/H/J/L1-377[»]
1N4RX-ray2.80B/D/F/H/J/L1-377[»]
1N4SX-ray2.60B/D/F/H/J/L1-377[»]
1S64X-ray2.55B/D/F/H/J/L1-377[»]
1TNBX-ray2.85B/D/F/H/J/L1-377[»]
1TNOX-ray2.70B/D/F/H/J/L1-377[»]
1TNUX-ray2.70B/D/F/H/J/L1-377[»]
1TNYX-ray2.70B/D/F/H/J/L1-377[»]
1TNZX-ray2.90B/D/F/H/J/L1-377[»]
ProteinModelPortalP53610.
SMRP53610. Positions 18-363.
ModBaseSearch...

Protein-protein interaction databases

IntActP53610. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004723; ENSRNOP00000004723; ENSRNOG00000003541.
GeneID81746.
KEGGrno:81746.
UCSCNM_031082. rat.

Organism-specific databases

CTD5229.
RGD621754. Pggt1b.

Phylogenomic databases

eggNOGroNOG07172.
GeneTreeENSGT00530000063392.
HOVERGENHBG008181.
InParanoidP53610.
OMAHGGTTFC.
OrthoDBEOG4KD6MC.
PhylomeDBP53610.

Gene expression databases

ArrayExpressP53610.
GenevestigatorP53610.
GermOnlineENSRNOG00000003541. Rattus norvegicus.

Family and domain databases

InterProIPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
KOK11713.
PfamPF00432. Prenyltrans. 4 hits.
[Graphical view]
SUPFAMSSF48239. Terp_cyc_toroid. 1 hit.
ProtoNetSearch...

Other

NextBio615482.

Entry information

Entry namePGTB1_RAT
AccessionPrimary (citable) accession number: P53610
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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