Identification |
---|
Name: | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase |
---|
Synonyms: | - Polyprenyl p-hydroxybenzoate decarboxylase
|
---|
Gene Name: | ubiD |
---|
Enzyme Class: | |
---|
Biological Properties |
---|
General Function: | Involved in carboxy-lyase activity |
---|
Specific Function: | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol |
---|
Cellular Location: | Cell membrane; Peripheral membrane protein (Probable) |
---|
SMPDB Pathways: | - Secondary Metabolites: Ubiquinol biosynthesis PW000981
- Secondary Metabolites: Ubiquinol biosynthesis 2 PW002036
|
---|
KEGG Pathways: | - Metabolic pathways eco01100
- Ubiquinone and other terpenoid-quinone biosynthesis ec00130
|
---|
KEGG Reactions: | | | |
1.02-Polyprenylphenol | + | 1.0 | + | 1.0 | ↔ | 1.04-Hydroxy-3-polyprenylbenzoate | + | 1.0 |
| | | |
|
---|
EcoCyc Reactions: | |
---|
Metabolites: | |
---|
GO Classification: | Component |
---|
cell part | membrane | plasma membrane | Function |
---|
carbon-carbon lyase activity | carboxy-lyase activity | catalytic activity | lyase activity | Process |
---|
cellular metabolic process | coenzyme metabolic process | cofactor metabolic process | metabolic process | oxidoreduction coenzyme metabolic process | ubiquinone biosynthetic process | ubiquinone metabolic process |
|
---|
Gene Properties |
---|
Blattner: | b3843 |
---|
Gene Orientation | Clockwise |
---|
Centisome Percentage: | 86.71 |
---|
Left Sequence End | 4023011 |
---|
Right Sequence End | 4024504 |
---|
Gene Sequence: | >1494 bp
ATGGACGCCATGAAATATAACGATTTACGCGACTTCTTGACGCTGCTTGAACAGCAGGGT
GAGCTAAAACGTATCACGCTCCCGGTGGATCCGCATCTGGAAATCACTGAAATTGCTGAC
CGCACTTTGCGTGCCGGTGGGCCTGCGCTGTTGTTCGAAAACCCTAAAGGCTACTCAATG
CCGGTGCTGTGCAACCTGTTCGGTACGCCAAAGCGCGTGGCGATGGGCATGGGGCAGGAA
GATGTTTCGGCGCTGCGTGAAGTTGGTAAATTATTGGCGTTTCTGAAAGAGCCGGAGCCG
CCAAAAGGTTTCCGCGACCTGTTTGATAAACTGCCGCAGTTTAAGCAAGTATTGAACATG
CCGACAAAGCGGCTGCGTGGTGCGCCCTGCCAACAAAAAATCGTCTCTGGCGATGACGTC
GATCTCAATCGCATTCCCATTATGACCTGCTGGCCGGAAGATGCCGCGCCGCTGATTACC
TGGGGGCTGACAGTGACGCGCGGCCCACATAAAGAGCGGCAGAATCTGGGCATTTATCGC
CAGCAGCTGATTGGTAAAAACAAACTGATTATGCGCTGGCTGTCGCATCGCGGCGGCGCG
CTGGATTATCAGGAGTGGTGTGCGGCGCATCCGGGCGAACGTTTCCCGGTTTCTGTGGCG
CTGGGTGCCGATCCCGCCACGATTCTCGGTGCAGTCACTCCCGTTCCGGATACGCTTTCA
GAGTATGCGTTTGCCGGATTGCTACGTGGCACCAAGACCGAAGTGGTGAAGTGTATCTCC
AATGATCTTGAAGTGCCCGCCAGTGCGGAGATTGTGCTGGAAGGGTATATCGAACAAGGC
GAAACTGCGCCGGAAGGGCCGTATGGCGACCACACCGGTTACTATAATGAAGTCGATAGT
TTCCCGGTATTTACCGTGACGCATATTACCCAGCGTGAAGATGCGATTTACCATTCCACC
TATACCGGGCGTCCGCCAGATGAGCCCGCGGTGCTGGGTGTCGCACTGAACGAAGTGTTT
GTGCCGATTCTGCAAAAACAGTTCCCGGAAATTGTCGATTTTTACCTGCCGCCGGAAGGC
TGCTCTTATCGCCTGGCGGTAGTGACAATCAAAAAACAGTACGCCGGACACGCGAAGCGC
GTCATGATGGGCGTCTGGTCGTTCTTACGCCAGTTTATGTACACTAAATTTGTGATCGTT
TGCGATGATGACGTTAACGCACGCGACTGGAACGATGTGATTTGGGCGATTACCACCCGT
ATGGACCCGGCGCGGGATACTGTTCTGGTAGAAAATACGCCTATTGATTATCTGGATTTT
GCCTCGCCTGTCTCCGGGCTGGGTTCAAAAATGGGGCTGGATGCCACGAATAAATGGCCG
GGGGAAACCCAGCGTGAATGGGGACGTCCCATCAAAAAAGATCCAGATGTTGTCGCGCAT
ATTGACGCCATCTGGGATGAACTGGCTATTTTTAACAACGGTAAAAGCGCCTGA |
---|
Protein Properties |
---|
Pfam Domain Function: | |
---|
Protein Residues: | 497 |
---|
Protein Molecular Weight: | 55603 |
---|
Protein Theoretical pI: | 5 |
---|
Signaling Regions: | |
---|
Transmembrane Regions: | |
---|
Protein Sequence: | >3-octaprenyl-4-hydroxybenzoate carboxy-lyase
MDAMKYNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENPKGYSM
PVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKEPEPPKGFRDLFDKLPQFKQVLNM
PTKRLRGAPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNLGIYR
QQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGADPATILGAVTPVPDTLS
EYAFAGLLRGTKTEVVKCISNDLEVPASAEIVLEGYIEQGETAPEGPYGDHTGYYNEVDS
FPVFTVTHITQREDAIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEG
CSYRLAVVTIKKQYAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTR
MDPARDTVLVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETQREWGRPIKKDPDVVAH
IDAIWDELAIFNNGKSA |
---|
References |
---|
External Links: | |
---|
General Reference: | - Bailey, M. J., Koronakis, V., Schmoll, T., Hughes, C. (1992). "Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes." Mol Microbiol 6:1003-1012. Pubmed: 1584020
- 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
- Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
- 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
- Leppik, R. A., Young, I. G., Gibson, F. (1976). "Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase." Biochim Biophys Acta 436:800-810. Pubmed: 782527
- Zhang, H., Javor, G. T. (2000). "Identification of the ubiD gene on the Escherichia coli chromosome." J Bacteriol 182:6243-6246. Pubmed: 11029449
|
---|