Difference between revisions of "Part:BBa K1080004"
 
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<partinfo>BBa_K1080004 short</partinfo>
 
<partinfo>BBa_K1080004 short</partinfo>
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<br><b> Mg protoporphyrin IX S-adenosyl methionine O-methyl transferase </b> - Magnesium-protoporphyrin O-methyltransferase (ChlM) [<html><a href="http://www.ncbi.nlm.nih.gov/pubmed/12828371">PMID: 12828371</a></html>; <html><a href="http://www.ncbi.nlm.nih.gov/pubmed/12489983">12489983</a></html>; <html><a href="http://www.ncbi.nlm.nih.gov/pubmed/4436384">4436384</a></html>]; ChloroP 1.1 predicts cp location  
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<br><b> Mg protoporphyrin IX S-adenosyl methionine O-methyl transferase </b> - Magnesium-protoporphyrin O-methyltransferase (chlM) [<html><a href="http://www.ncbi.nlm.nih.gov/pubmed/12828371">PMID: 12828371</a></html>; <html><a href="http://www.ncbi.nlm.nih.gov/pubmed/12489983">12489983</a></html>; <html><a href="http://www.ncbi.nlm.nih.gov/pubmed/4436384">4436384</a></html>]; ChloroP 1.1 predicts cp location  
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<br>
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<!-- Add more about the biology of this part here
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===Usage and Biology===
 
===Usage and Biology===
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ChlM is responsible for the methylation of magnesium protoporphyrin IX. It encodes the enzyme Mg-protoporphyrin IX methyltransferase, to facilitate a highly regulated process in catalyzing magnesium chelatase [http://www.ncbi.nlm.nih.gov/pubmed/17135235]. The main reaction catalyzed by ChlM is the transfer of the methyl group from S-adenosylmethionine to the carboxyl group of the C13 propionate side chain of magnesium protoporphyrin IX [http://www.ncbi.nlm.nih.gov/pubmed/25077963]. This reaction is one of the most important steps in chlorophyll biosynthesis from protoporphyrin IX.
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<br>
  
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K1080004 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1080004 SequenceAndFeatures</partinfo>
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<br>
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<br>
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<br>
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<b> Amino Acid Sequence </b>
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<FONT FACE="courier">MASEIAQTAD VGSLTFAVGG VGAVVGLGAL LVATDHQKRR SEQMKSFDGD EKEAVKDYFN<br> TAGFERWRKI YGETDEVNKV QLDIRTGHAQ TVDKVLRWVD EEGSVQGITV ADCGCGTGSL<br> AIQLALRGAA VSASDISAAM ASEAEQRYQQ AVAAGQGKAP KVAPKFEALD LESVKGKYDT<br> VTCLDVMIHY PQDKVDAMIT HLAGLSDRRL IISFAPKTLS YSILKRIGEL FPGPSKATRA<br> YLHREEDVEA ALKRAGFKVT KREMTATSFY FSRLLEAIRE </FONT>
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 +
References and documentation are available.
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Please note the modified algorithm for extinction coefficient.
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 +
--------------------------------------------------------------------------------
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Number of amino acids: 280
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 +
Molecular weight: 30440.6
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Theoretical pI: 6.25
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Amino acid composition:
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<br>
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Ala (A)  36 12.9%<br>
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Arg (R)  17   6.1%<br>
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Asn (N)  2   0.7%<br>
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Asp (D)  18   6.4%<br>
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Cys (C)  3   1.1%<br>
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Gln (Q)  12   4.3%<br>
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Glu (E)  20   7.1%<br>
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Gly (G)  23   8.2%<br>
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His (H)  5   1.8%<br>
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Ile (I)  13   4.6%<br>
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Leu (L)  22   7.9%<br>
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Lys (K)  19   6.8%<br>
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Met (M)  6   2.1%<br>
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Phe (F)  10   3.6%<br>
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Pro (P)  6   2.1%<br>
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Ser (S)  18   6.4%<br>
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Thr (T)  17   6.1%<br>
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Trp (W)  2   0.7%<br>
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Tyr (Y)  8   2.9%<br>
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Val (V)  23   8.2%<br>
 +
Pyl (O)  0   0.0%<br>
 +
Sec (U)  0   0.0%<br>
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 +
(B)  0   0.0%
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(Z)  0   0.0%
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(X)  0   0.0%
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 +
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Total number of negatively charged residues (Asp + Glu): 38
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Total number of positively charged residues (Arg + Lys): 36
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Atomic composition:
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Carbon      C       1340
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Hydrogen    H       2150
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Nitrogen    N       376
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Oxygen      O       414
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Sulfur      S         9
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Formula: C1340H2150N376O414S9
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Total number of atoms: 4289
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Extinction coefficients:
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Extinction coefficients are in units of  M-1 cm-1, at 280 nm measured in water.
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Ext. coefficient    23045
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Abs 0.1% (=1 g/l)  0.757, assuming all pairs of Cys residues form cystines
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Ext. coefficient    22920
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Abs 0.1% (=1 g/l)  0.753, assuming all Cys residues are reduced
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Estimated half-life:
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The N-terminal of the sequence considered is M (Met).
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The estimated half-life is:
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                            30 hours (mammalian reticulocytes, in vitro).
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                            >20 hours (yeast, in vivo).
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                            >10 hours (Escherichia coli, in vivo).
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Instability index:
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The instability index (II) is computed to be 34.88
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This classifies the protein as stable.
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Aliphatic index: 85.43
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Grand average of hydropathicity (GRAVY): -0.198
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SIB Swiss Institute of Bioinformatics | Disclaimer
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===Source===
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<i>Chlamydomonas reinhardtii</i>
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===References===
  
  

Latest revision as of 01:10, 17 October 2014

ChlM
Mg protoporphyrin IX S-adenosyl methionine O-methyl transferase - Magnesium-protoporphyrin O-methyltransferase (ChlM) [PMID: 12828371; 12489983; 4436384]; ChloroP 1.1 predicts cp location

Usage and Biology

ChlM is responsible for the methylation of magnesium protoporphyrin IX. It encodes the enzyme Mg-protoporphyrin IX methyltransferase, to facilitate a highly regulated process in catalyzing magnesium chelatase [http://www.ncbi.nlm.nih.gov/pubmed/17135235]. The main reaction catalyzed by ChlM is the transfer of the methyl group from S-adenosylmethionine to the carboxyl group of the C13 propionate side chain of magnesium protoporphyrin IX [http://www.ncbi.nlm.nih.gov/pubmed/25077963]. This reaction is one of the most important steps in chlorophyll biosynthesis from protoporphyrin IX.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 230
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]




Amino Acid Sequence

MASEIAQTAD VGSLTFAVGG VGAVVGLGAL LVATDHQKRR SEQMKSFDGD EKEAVKDYFN
TAGFERWRKI YGETDEVNKV QLDIRTGHAQ TVDKVLRWVD EEGSVQGITV ADCGCGTGSL
AIQLALRGAA VSASDISAAM ASEAEQRYQQ AVAAGQGKAP KVAPKFEALD LESVKGKYDT
VTCLDVMIHY PQDKVDAMIT HLAGLSDRRL IISFAPKTLS YSILKRIGEL FPGPSKATRA
YLHREEDVEA ALKRAGFKVT KREMTATSFY FSRLLEAIRE

References and documentation are available. Please note the modified algorithm for extinction coefficient.

Number of amino acids: 280

Molecular weight: 30440.6

Theoretical pI: 6.25

Amino acid composition:
Ala (A) 36 12.9%
Arg (R) 17 6.1%
Asn (N) 2 0.7%
Asp (D) 18 6.4%
Cys (C) 3 1.1%
Gln (Q) 12 4.3%
Glu (E) 20 7.1%
Gly (G) 23 8.2%
His (H) 5 1.8%
Ile (I) 13 4.6%
Leu (L) 22 7.9%
Lys (K) 19 6.8%
Met (M) 6 2.1%
Phe (F) 10 3.6%
Pro (P) 6 2.1%
Ser (S) 18 6.4%
Thr (T) 17 6.1%
Trp (W) 2 0.7%
Tyr (Y) 8 2.9%
Val (V) 23 8.2%
Pyl (O) 0 0.0%
Sec (U) 0 0.0%

(B)   0	  0.0%
(Z)   0	  0.0%
(X)   0	  0.0%


Total number of negatively charged residues (Asp + Glu): 38 Total number of positively charged residues (Arg + Lys): 36

Atomic composition:

Carbon C 1340 Hydrogen H 2150 Nitrogen N 376 Oxygen O 414 Sulfur S 9

Formula: C1340H2150N376O414S9 Total number of atoms: 4289

Extinction coefficients:

Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.

Ext. coefficient 23045 Abs 0.1% (=1 g/l) 0.757, assuming all pairs of Cys residues form cystines


Ext. coefficient 22920 Abs 0.1% (=1 g/l) 0.753, assuming all Cys residues are reduced

Estimated half-life:

The N-terminal of the sequence considered is M (Met).

The estimated half-life is: 

                            30 hours (mammalian reticulocytes, in vitro).
                           >20 hours (yeast, in vivo).
                           >10 hours (Escherichia coli, in vivo).


Instability index:

The instability index (II) is computed to be 34.88 This classifies the protein as stable.


Aliphatic index: 85.43

Grand average of hydropathicity (GRAVY): -0.198


SIB Swiss Institute of Bioinformatics | Disclaimer

Source

Chlamydomonas reinhardtii

References