MG_263 – Cof-like hydrolase
Name | ||
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WID | MG_263 |
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Name | Cof-like hydrolase |
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Protein product | MG_263_MONOMER | |
Cross references | GenBank: AAC71485.1, BioCyc: MG_263, CMR: MG_263, SwissProt: P47505 | |
Homologs | ||
Classification | ||
Type | mRNA |
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Structure | ||
Structure |
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Sequence | Chromosome: Mgenitalium_Chr_1, Coordinate: 320177 (nt), Length: 876 (nt), Direction: Forward, G/C content: 31.4%, Sequence: 1 51 101 151 201 251 301 351 401 451 501 551 601 651 701 751 801 851 ATGAAAAACGAAATTAAATATCTTTATTCTGACTTGGATGGTACTATTGT TAGCTGAAATCCTAAAACAGAATTTGTTTATCAAAATAAAAGTTATAAAA ATTTCCATGAAGTTAGTGATGCTACTATTAGTGCTTTTTACCGATTGCAA CAAAAGGGAATTAAGGTTGGTATTGTTACTGGTAGGGATTATTGTCGGGT GTTATGACTTGAAAAACAACTTAGAACAGGATTGCCTACCATTACTTTAG ATGGGGCTATTATCTTTTATCAAAACGAAATCTTAAGTCAAACTTATTTA GATGATAGATTTATTGAAGGGATTAATAACATAGTAAAGCGCTTTCCTGA AGCTGCTTATAAACTTAACAGTGGTTGAATTAGTTACTTTACTAAAAACC CTTCTGTTATCTTTGAAATTGATTATGCTTTTCTTGGCTATTTCAACCCT AACACCAAACTACAAAAAAAGTTTATAGACAGTACTGAAAATTGAGATCT TAATAAACTAAAAGTTAATCAGGTTTACTTTGATATTGATACTTGCCCCT TAGCAATGCAAAAGGAAATAATTGAACTAATTAGTGTTAGTGATGTAAAT GCCAAAATCTATGAGCACTCTATGTACATTATTAAAAATGGTGTTTCTAA AGCTAGTGCATTGCAAAGCCTTAACCAGTTTGCAATTCCAATAACAAAAG ATAACACTATTGTTTGTGGGGATGGAGATAATGACATTGAAATGATGCAG TGAGCTAAACACAGTGTCTCACTAATCGGTAGTAATCCCAAATGCTTTGC TCTAGCAAAATACCACACTGATAGTGTTGACAATGATGGTATTGCTAACT GGATTGAAAAAAACTTGTTATGTTAA 50 100 150 200 250 300 350 400 450 500 550 600 650 700 750 800 850 876 |
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Transcription unit | TU_174 |
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Empirical formula (pH 7.5) | H9347C8470N3510O6112P876 | |
Molecular weight (pH 7.5; Da) | 285236.37 |
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Functional genomics | ||
Is essential | Yes (Show evidence) |
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Relative expression | 0.851454 (dimensionless) (Show evidence) |
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Half life | 4.425 (min) (Show evidence) |
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Extinction coefficient (260 nm, 25C, pH 7.0) |
9062300 | |
pI | 4.03 | |
Comments | ||
Comments | HAD-like hydrolase superfamily [PUB_0096]; most HAD proteins have phosphatase activity [PUB_0108]; several HAD catalyze dehalogenase (C-halogen bond hydrolysis), phosphonatase (C-P bond hydrolysis), and ß-phosphoglucomutase (CO-P bond hydrolysis and intramolecular phosphoryl transfer) reactions [PUB_0108]; several additional functions have been annotated for HAD proteins -- lipopolysaccharide biosynthesis, degradation of 2-phosphoglycolate produced during DNA repair, biosynthesis of serine, detoxification, glycation repair to free proteins from the glycation products derived from direct nonenzymatic glycosylation [PUB_0108]; HAD phosphatases have broad and overlapping substrate spectra [PUB_0108]; none of the HAD proteins are essential in E. coli [PUB_0108]; | |
References |
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Metadata | ||
Created | 2012-10-01 15:07:21 | |
Last updated | 2012-10-01 15:13:17 |