Identification
Name:Protoheme IX farnesyltransferase
Synonyms:
  • Heme B farnesyltransferase
  • Heme O synthase
Gene Name:cyoE
Enzyme Class:Not Available
Biological Properties
General Function:Involved in protoheme IX farnesyltransferase activity
Specific Function:Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Farnesyl pyrophosphate+1.0Thumb1.0Thumb+1.0Pyrophosphate
1.0ferroheme b + 1.0Water + 1.0Farnesyl pyrophosphate + 1.0Farnesyl pyrophosphate → 1.0Heme O + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00961Farnesyl pyrophosphateMetaboCard
ECMDB24252ferroheme bMetaboCard
ECMDB03178HemeMetaboCard
ECMDB01162Heme OMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
catalytic activity
farnesyltranstransferase activity
prenyltransferase activity
protoheme IX farnesyltransferase activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
heme biosynthetic process
heme O biosynthetic process
metabolic process
nitrogen compound metabolic process
porphyrin biosynthetic process
porphyrin metabolic process
tetrapyrrole metabolic process
Gene Properties
Blattner:b0428
Gene OrientationCounterclockwise
Centisome Percentage:9.61
Left Sequence End446039
Right Sequence End446929
Gene Sequence:
>891 bp
ATGAGCGGCTTACCTCTTATTTCGCGCCGTCGACTGTTAACGGCGATGGCGCTTTCTCCG
TTGTTATGGCAGATGAATACCGCCCACGCGGCGGCTATTGATCCCAATCGTATTGTGGCG
CTGGAGTGGTTGCCGGTGGAATTACTGCTGGCGCTCGGCATCGTGCCTTACGGCGTGGCG
GATACCATCAACTATCGCCTGTGGGTCAGCGAACCACCATTGCCGGACTCAGTGATCGAC
GTCGGTTTGCGCACAGAACCTAACCTTGAACTGCTGACCGAAATGAAACCATCGTTTATG
GTCTGGTCGGCAGGATATGGCCCTTCACCAGAAATGCTGGCTCGTATTGCGCCGGGTCGC
GGATTTAACTTCAGTGACGGCAAACAGCCGTTGGCGATGGCGCGTAAATCGCTGACGGAA
ATGGCAGATTTACTTAACCTGCAAAGCGCAGCGGAAACGCATTTAGCGCAATATGAAGAC
TTTATCCGCAGCATGAAACCCCGCTTTGTGAAGCGTGGTGCGCGTCCGTTATTGCTGACG
ACGCTTATCGATCCGCGCCATATGCTGGTCTTCGGTCCAAACAGCTTGTTCCAGGAAATT
CTTGATGAGTACGGCATCCCAAATGCCTGGCAAGGGGAAACCAACTTCTGGGGCAGTACC
GCCGTCAGTATCGATCGTCTGGCGGCGTATAAAGACGTTGATGTGCTCTGTTTTGATCAC
GACAACAGCAAAGACATGGATGCGCTAATGGCAACGCCGCTGTGGCAGGCCATGCCGTTT
GTCCGCGCCGGACGCTTTCAGCGCGTACCTGCAGTCTGGTTTTATGGTGCGACGCTCTCG
GCAATGCACTTTGTGCGCGTTCTGGATAACGCCATCGGAGGTAAAGCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:296
Protein Molecular Weight:32248
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 10-28
  • 38-56
  • 79-97
  • 108-126
  • 198-216
  • 229-247
  • 269-287
Protein Sequence:
>Protoheme IX farnesyltransferase
MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYI
DRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVY
VGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSYAI
AIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAV
SVWWLGMALRGYKVADDRIWARKLFGFSIIAITALSVMMSVDFMVPDSHTLLAAVW
References
External Links:
ResourceLink
Uniprot ID:P0AEA5
Uniprot Name:CYOE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674358
Ecogene ID:EG10182
Ecocyc:EG10182
ColiBase:b0428
Kegg Gene:b0428
EchoBASE ID:EB0179
CCDB:CYOE_ECOLI
BacMap:16128413
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Chepuri, V., Gennis, R. B. (1990). "The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli." J Biol Chem 265:12978-12986. Pubmed: 2165491
  • Chepuri, V., Lemieux, L., Au, D. C., Gennis, R. B. (1990). "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem 265:11185-11192. Pubmed: 2162835
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Saiki, K., Mogi, T., Anraku, Y. (1992). "Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase." Biochem Biophys Res Commun 189:1491-1497. Pubmed: 1336371
  • Saiki, K., Mogi, T., Hori, H., Tsubaki, M., Anraku, Y. (1993). "Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli." J Biol Chem 268:26927-26934. Pubmed: 8262927
  • Saiki, K., Mogi, T., Ogura, K., Anraku, Y. (1993). "In vitro heme O synthesis by the cyoE gene product from Escherichia coli." J Biol Chem 268:26041-26044. Pubmed: 8253713