Identification |
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Name: | Bifunctional glutathionylspermidine synthetase/amidase |
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Synonyms: | - Glutathionylspermidine synthase
- GSP synthetase
- Glutathione:spermidine ligase [ADP-forming]
- Glutathionylspermidine amidase
- Glutathionylspermidine amidohydrolase [spermidine-forming]
- GSP amidase
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Gene Name: | gsp |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Amino acid transport and metabolism |
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Specific Function: | Catalyzes the formation of an amide bond between glutathione and spermidine coupled with hydrolysis of ATP; also catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine |
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Cellular Location: | Not Available |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 | + | 1.0 |
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Complex Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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Metabolites: | |
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GO Classification: | Not Available |
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Gene Properties |
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Blattner: | b2988 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 67.56 |
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Left Sequence End | 3134685 |
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Right Sequence End | 3136544 |
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Gene Sequence: | >1860 bp
ATGAGCAAAGGAACGACCAGCCAGGATGCCCCGTTCGGGACATTATTGGGCTACGCCCCA
GGTGGGGTAGCAATCTACTCTTCAGATTACAGTTCTCTCGATCCGCAGGAATACGAAGAT
GACGCCGTATTCCGTAGCTATATCGACGACGAATATATGGGCCACAAGTGGCAATGCGTT
GAATTTGCTCGCCGTTTTCTCTTTCTGAATTACGGTGTGGTCTTTACTGACGTGGGTATG
GCGTGGGAGATTTTCTCGCTGCGCTTCCTGCGAGAAGTGGTTAATGACAACATCCTGCCA
TTGCAGGCATTTCCTAACGGCTCGCCGCGTGCGCCGGTCGCGGGTGCGCTTCTTATCTGG
GATAAAGGCGGTGAATTTAAAGACACTGGCCATGTCGCCATCATTACCCAATTGCATGGC
AACAAAGTCCGTATTGCGGAACAGAACGTGATTCATTCCCCGTTGCCGCAAGGGCAACAG
TGGACGCGCGAGCTGGAGATGGTGGTCGAAAACGGCTGCTATACCCTGAAAGACACTTTT
GATGACACCACCATTCTGGGCTGGATGATCCAGACGGAAGATACTGAATACAGCTTACCG
CAGCCGGAAATTGCAGGCGAGCTGCTGAAAATCAGCGGAGCGCGCCTGGAAAACAAAGGC
CAGTTTGACGGTAAATGGCTGGATGAAAAAGATCCGCTGCAAAACGCCTATGTGCAGGCC
AACGGTCAGGTGATCAATCAGGATCCTTATCATTACTACACCATTACCGAGAGTGCCGAG
CAGGAGCTAATTAAAGCCACCAACGAGCTGCACCTGATGTATCTTCACGCAACCGACAAG
GTGCTGAAAGATGACAACCTGCTGGCGCTGTTCGACATCCCGAAAATCCTCTGGCCACGT
TTGCGTCTCTCCTGGCAGCGTCGCCGTCACCATATGATCACTGGTCGTATGGATTTCTGC
ATGGATGAGCGTGGCCTGAAGGTTTACGAGTACAACGCCGACTCCGCCTCCTGTCATACC
GAAGCGGGCTTGATCCTCGAACGTTGGGCGGAGCAGGGCTATAAAGGCAACGGCTTCAAT
CCGGCGGAAGGGCTGATTAACGAATTGGCTGGTGCCTGGAAACACAGTCGTGCACGTCCG
TTTGTCCATATCATGCAGGACAAAGATATCGAGGAAAACTATCACGCGCAGTTTATGGAG
CAGGCGCTGCACCAGGCGGGCTTTGAAACGCGTATCTTGCGTGGATTGGATGAACTGGGC
TGGGATGCTGCCGGGCAACTGATTGATGGGGAAGGGCGACTGGTTAACTGCGTGTGGAAA
ACCTGGGCGTGGGAAACCGCGTTTGATCAGATTCGTGAAGTTAGCGACCGTGAGTTTGCT
GCGGTGCCAATCCGTACCGGTCATCCGCAAAACGAAGTGCGTCTTATCGACGTATTGCTG
CGCCCGGAAGTGCTGGTCTTTGAGCCGCTGTGGACGGTGATCCCCGGCAACAAAGCGATT
CTGCCGATCCTCTGGTCGCTGTTCCCGCACCATCGTTACCTGCTGGATACCGATTTCACT
GTTAATGATGAACTGGTGAAAACAGGTTACGCAGTGAAACCGATCGCCGGTCGCTGTGGC
AGCAATATCGACCTCGTCAGCCATCATGAAGAGGTGCTGGACAAAACCAGCGGTAAATTT
GCCGAGCAGAAAAACATCTATCAGCAACTGTGGTGTTTGCCGAAAGTGGACGGTAAATAC
ATTCAGGTATGTACCTTCACCGTTGGCGGCAACTACGGTGGGACGTGTTTGCGCGGTGAT
GAATCACTGGTCATCAAAAAAGAGAGTGATATTGAACCGTTAATTGTGGTGAAAAAGTAA
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 619 |
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Protein Molecular Weight: | 70531 |
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Protein Theoretical pI: | 5 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Bifunctional glutathionylspermidine synthetase/amidase
MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCV
EFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIW
DKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTF
DDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQA
NGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPR
LRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFN
PAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELG
WDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLL
RPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCG
SNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGD
ESLVIKKESDIEPLIVVKK |
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References |
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External Links: | |
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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
- Bollinger, J. M. Jr, Kwon, D. S., Huisman, G. W., Kolter, R., Walsh, C. T. (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase." J Biol Chem 270:14031-14041. Pubmed: 7775463
- 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
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