Putative acyl-CoA thioester hydrolase ybhC (P46130)

Identification
Name:Putative acyl-CoA thioester hydrolase ybhC
Synonyms:Not Available
Gene Name:ybhC
Enzyme Class:
Biological Properties
General Function:Involved in pectinesterase activity
Specific Function:Putative thioesterase. Does not bind pectin, and has no pectinesterase activity
Cellular Location:Cell outer membrane; Lipid-anchor (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Lyxose + 1.0Water ↔ 1.0Methanol + 1.0Pectic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Pectin + 1.0Water ↔ 1.0Methanol + 1.0Pectic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04097L-LyxoseMetaboCard
ECMDB01875MethanolMetaboCard
ECMDB21445Pectic acidMetaboCard
ECMDB23834PectinMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cell wall
external encapsulating structure
Function
carboxylesterase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
pectinesterase activity
Process
cell wall modification
cell wall organization
cell wall organization or biogenesis
cellular component organization or biogenesis
Gene Properties
Blattner:b0772
Gene OrientationCounterclockwise
Centisome Percentage:17.36
Left Sequence End805221
Right Sequence End806504
Gene Sequence:
>1284 bp
GTGTCGAATAACGCTTTACAAACAATTATTAACGCCCGGTTACCAGGCGAAGAGGGGCTG
TGGCAGATTCATCTGCAGGACGGAAAAATCAGCGCCATTGATGCGCAATCCGGCGTGATG
CCCATAACTGAAAACAGCCTGGATGCCGAACAAGGTTTAGTTATACCGCCGTTTGTGGAG
CCACATATTCACCTGGACACCACGCAAACCGCCGGACAACCGAACTGGAATCAGTCCGGC
ACGCTGTTTGAAGGCATTGAACGCTGGGCCGAGCGCAAAGCGTTATTAACCCATGACGAT
GTGAAACAACGCGCATGGCAAACGCTGAAATGGCAGATTGCCAACGGCATTCAGCATGTG
CGTACCCATGTCGATGTTTCGGATGCAACGCTAACTGCGCTGAAAGCAATGCTGGAAGTG
AAGCAGGAAGTCGCGCCGTGGATTGATCTGCAAATCGTCGCCTTCCCTCAGGAAGGGATT
TTGTCGTATCCCAACGGTGAAGCGTTGCTGGAAGAGGCGTTACGCTTAGGGGCAGATGTA
GTGGGGGCGATTCCGCATTTTGAATTTACCCGTGAATACGGCGTGGAGTCGCTGCATAAA
ACCTTCGCCCTGGCGCAAAAATACGACCGTCTCATCGACGTTCACTGTGATGAGATCGAT
GACGAGCAGTCGCGCTTTGTCGAAACCGTTGCTGCCCTGGCGCACCATGAAGGCATGGGC
GCGCGAGTCACCGCCAGCCACACCACGGCAATGCACTCCTATAACGGGGCGTATACCTCA
CGCCTGTTCCGCTTGCTGAAAATGTCCGGTATTAACTTTGTCGCCAACCCGCTGGTCAAT
ATTCATCTGCAAGGACGTTTCGATACGTATCCAAAACGTCGCGGCATCACGCGCGTTAAA
GAGATGCTGGAGTCCGGCATTAACGTCTGCTTTGGTCACGATGATGTCTTCGATCCGTGG
TATCCGCTGGGAACGGCGAATATGCTGCAAGTGCTGCATATGGGGCTGCATGTTTGCCAG
TTGATGGGCTACGGGCAGATTAACGATGGCCTGAATTTAATCACCCACCACAGCGCAAGG
ACGTTGAATTTGCAGGATTACGGCATTGCCGCCGGAAACAGCGCCAACCTGATTATCCTG
CCGGCTGAAAATGGGTTTGATGCGCTGCGCCGTCAGGTTCCGGTACGTTATTCGGTACGT
GGCGGCAAGGTGATTGCCAGCACACAACCGGCACAAACCACCGTATATCTGGAGCAGCCA
GAAGCCATCGATTACAAACGTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:427
Protein Molecular Weight:46082
Protein Theoretical pI:6
Signaling Regions:
  • 1-21
Transmembrane Regions:
  • None
Protein Sequence:
>Putative acyl-CoA thioester hydrolase ybhC
MNTFSVSRLALALAFGVTLTACSSTPPDQRPSDQTAPGTSSRPILSAKEAQNFDAQHYFA
SLTPGAAAWNPSPITLPAQPDFVVGPAGTQGVTHTTIQAAVDAAIIKRTNKRQYIAVMPG
EYQGTVYVPAAPGGITLYGTGEKPIDVKIGLSLDGGMSPADWRHDVNPRGKYMPGKPAWY
MYDSCQSKRSDSIGVLCSAVFWSQNNGLQLQNLTIENTLGDSVDAGNHPAVALRTDGDQV
QINNVNILGRQNTFFVTNSGVQNRLETNRQPRTLVTNSYIEGDVDIVSGRGAVVFDNTEF
RVVNSRTQQEAYVFAPATLSNIYYGFLAVNSRFNAFGDGVAQLGRSLDVDANTNGQVVIR
DSAINEGFNTAKPWADAVISNRPFAGNTGSVDDNDEIQRNLNDTNYNRMWEYNNRGVGSK
VVAEAKK
References
External Links:
ResourceLink
Uniprot ID:P46130
Uniprot Name:YBHC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674479
Ecogene ID:EG12875
Ecocyc:EG12875
ColiBase:b0772
Kegg Gene:b0772
EchoBASE ID:EB2713
CCDB:YBHC_ECOLI
BacMap:16128740
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
  • Borodovsky, M., McIninch, J. D., Koonin, E. V., Rudd, K. E., Medigue, C., Danchin, A. (1995). "Detection of new genes in a bacterial genome using Markov models for three gene classes." Nucleic Acids Res 23:3554-3562. Pubmed: 7567469
  • Eklof, J. M., Tan, T. C., Divne, C., Brumer, H. (2009). "The crystal structure of the outer membrane lipoprotein YbhC from Escherichia coli sheds new light on the phylogeny of carbohydrate esterase family 8." Proteins 76:1029-1036. Pubmed: 19452549
  • 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
  • Kuznetsova, E., Proudfoot, M., Sanders, S. A., Reinking, J., Savchenko, A., Arrowsmith, C. H., Edwards, A. M., Yakunin, A. F. (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29:263-279. Pubmed: 15808744
  • Landy, A., Ross, W. (1977). "Viral integration and excision: structure of the lambda att sites." Science 197:1147-1160. Pubmed: 331474
  • Molloy, M. P., Herbert, B. R., Slade, M. B., Rabilloud, T., Nouwens, A. S., Williams, K. L., Gooley, A. A. (2000). "Proteomic analysis of the Escherichia coli outer membrane." Eur J Biochem 267:2871-2881. Pubmed: 10806384
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232