MG_263 – Cof-like hydrolase

Name
WID MG_263 View in model
Name Cof-like hydrolase View in model
Protein product MG_263_MONOMER
Cross references GenBank: AAC71485.1, CMR: MG_263, BioCyc: MG_263, SwissProt: P47505
Homologs
 
Classification
Type mRNA View in model
 
Structure
Structure 317677323553 MG_261 MG_262 MG_263 MG_264 MG_265 MG_266 MG_498 View in model
Sequence Chromosome: Mgenitalium_Chr_1, Coordinate: 320177 (nt), Length: 876 (nt), Direction: Forward, G/C content: 31.4%, Sequence:
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ATGAAAAACGAAATTAAATATCTTTATTCTGACTTGGATGGTACTATTGT
TAGCTGAAATCCTAAAACAGAATTTGTTTATCAAAATAAAAGTTATAAAA
ATTTCCATGAAGTTAGTGATGCTACTATTAGTGCTTTTTACCGATTGCAA
CAAAAGGGAATTAAGGTTGGTATTGTTACTGGTAGGGATTATTGTCGGGT
GTTATGACTTGAAAAACAACTTAGAACAGGATTGCCTACCATTACTTTAG
ATGGGGCTATTATCTTTTATCAAAACGAAATCTTAAGTCAAACTTATTTA
GATGATAGATTTATTGAAGGGATTAATAACATAGTAAAGCGCTTTCCTGA
AGCTGCTTATAAACTTAACAGTGGTTGAATTAGTTACTTTACTAAAAACC
CTTCTGTTATCTTTGAAATTGATTATGCTTTTCTTGGCTATTTCAACCCT
AACACCAAACTACAAAAAAAGTTTATAGACAGTACTGAAAATTGAGATCT
TAATAAACTAAAAGTTAATCAGGTTTACTTTGATATTGATACTTGCCCCT
TAGCAATGCAAAAGGAAATAATTGAACTAATTAGTGTTAGTGATGTAAAT
GCCAAAATCTATGAGCACTCTATGTACATTATTAAAAATGGTGTTTCTAA
AGCTAGTGCATTGCAAAGCCTTAACCAGTTTGCAATTCCAATAACAAAAG
ATAACACTATTGTTTGTGGGGATGGAGATAATGACATTGAAATGATGCAG
TGAGCTAAACACAGTGTCTCACTAATCGGTAGTAATCCCAAATGCTTTGC
TCTAGCAAAATACCACACTGATAGTGTTGACAATGATGGTATTGCTAACT
GGATTGAAAAAAACTTGTTATGTTAA
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876
View in model
Transcription unit TU_174 View in model
Empirical formula (pH 7.5) H9347C8470N3510O6112P876
Molecular weight (pH 7.5; Da) 285236.37 View in model
 
Functional genomics
Is essential
Yes (Show evidence)
View in model
Relative expression
0.851454 (dimensionless) (Show evidence)
View in model
Half life
4.425 (min) (Show evidence)
View in model
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
  1. Bernstein JA, Khodursky AB, Lin PH, Lin-Chao S, Cohen SN. Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays. Proc Natl Acad Sci U S A 99, 9697-702 (2002). WholeCell: PUB_0602, PubMed: 12119387

  2. Glass JI, Assad-Garcia N, Alperovich N, Yooseph S, Lewis MR, Maruf M, Hutchison CA 3rd, Smith HO, Venter JC. Essential genes of a minimal bacterium. Proc Natl Acad Sci U S A 103, 425-30 (2006). WholeCell: PUB_0193, PubMed: 16407165

  3. Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem 281, 36149-61 (2006). WholeCell: PUB_0108, PubMed: 16990279

  4. UniProt Consortium. The Universal Protein Resource (UniProt) 2009. Nucleic Acids Res 37, D169-74 (2009). WholeCell: PUB_0096, PubMed: 18836194, URL: http://www.uniprot.org/uniprot/

  5. Weiner J 3rd, Zimmerman CU, Göhlmann HW, Herrmann R. Transcription profiles of the bacterium Mycoplasma pneumoniae grown at different temperatures. Nucleic Acids Res 31, 6306-20 (2003). WholeCell: PUB_0569, PubMed: 14576319

 
Metadata
Created 2012-10-01 15:07:21
Last updated 2012-10-01 15:13:17