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ECOLI:ISPA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ispA
Protein Name(s) Farnesyl diphosphate synthase

FPP synthase (2E,6E)-farnesyl diphosphate synthase Geranyltranstransferase

External Links
UniProt P22939
EMBL D00694
U82664
U00096
AP009048
PIR JQ0665
RefSeq NP_414955.1
YP_488713.1
PDB 1RQI
1RQJ
PDBsum 1RQI
1RQJ
ProteinModelPortal P22939
SMR P22939
DIP DIP-10044N
IntAct P22939
MINT MINT-1233182
STRING 511145.b0421
BindingDB P22939
ChEMBL CHEMBL1075078
SWISS-2DPAGE P22939
PaxDb P22939
PRIDE P22939
EnsemblBacteria AAC73524
BAE76201
GeneID 12930843
945064
KEGG ecj:Y75_p0409
eco:b0421
PATRIC 32115991
EchoBASE EB0503
EcoGene EG10508
eggNOG COG0142
HOGENOM HOG000009101
InParanoid P22939
KO K00795
OMA QNRINHF
OrthoDB EOG6TN43W
PhylomeDB P22939
BioCyc EcoCyc:FPPSYN-MONOMER
ECOL316407:JW0411-MONOMER
MetaCyc:FPPSYN-MONOMER
BRENDA 2.5.1.1
SABIO-RK P22939
EvolutionaryTrace P22939
PRO PR:P22939
Proteomes UP000000318
UP000000625
Genevestigator P22939
GO GO:0005737
GO:0004161
GO:0004337
GO:0046872
GO:0045337
GO:0033384
Gene3D 1.10.600.10
InterPro IPR000092
IPR017446
IPR008949
PANTHER PTHR12001
Pfam PF00348
SUPFAM SSF48576
PROSITE PS00723
PS00444

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0045337

farnesyl diphosphate biosynthetic process

PMID:2676985[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0033384

geranyl diphosphate biosynthetic process

PMID:15809342[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004337

geranyltranstransferase activity

PMID:15721807[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004161

dimethylallyltranstransferase activity

PMID:15721807[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008299

isoprenoid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000092

P

Seeded From UniProt

complete

enables

GO:0004337

geranyltranstransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.5.1.10

F

Seeded From UniProt

complete

involved_in

GO:0008299

isoprenoid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0414

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Fujisaki, S et al. (1989) Isolation and characterization of an Escherichia coli mutant having temperature-sensitive farnesyl diphosphate synthase. J. Bacteriol. 171 5654-8 PubMed GONUTS page
  2. Fujisaki, S et al. (2005) Disruption of the structural gene for farnesyl diphosphate synthase in Escherichia coli. J. Biochem. 137 395-400 PubMed GONUTS page
  3. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  4. 4.0 4.1 Lee, PC et al. (2005) Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity. Metab. Eng. 7 18-26 PubMed GONUTS page