Difference between revisions of "Part:BBa K1998010"

Latest revision as of 13:15, 21 October 2016

HydG

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

Overview

This part is composed of the hydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of hydE, hydF, and hydG. Within several prokaryotic genomes hydE, hydF, and hydG are found in putative operons with [Fe] hydrogenase structural genes.

Biology & Literature

hydG is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. hydG breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that hydG cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. hydE and hydF are maturases also required for the assembly of an active hydrogenase [3]. The binding site in hydG can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].

Protein information

hydG
Mass: 63.74kDa
Sequence:
MSVPLQCNAGRLLAGQRPCGVRARLNRRVCVPVTAHGKASATREYAGDFLPGTTISHAWSVERETHHRYRNPAEWINEAA IHKALETSKADAQDAGRVREILAKAKEKAFVTEHAPVNAESKSEFVQGLTLEECATLINVDSNNVELMNEIFDTALAIKE RIYGNRVVLFAPLYIANHCMNTCTYCAFRSANKGMERSILTDDDLREEVAALQRQGHRRILALTGEHPKYTFDNFLHAVN VIASVKTEPEGSIRRINVEIPPLSVSDMRRLKNTDSVGTFVLFQETYHRDTFKVMHPSGPKSDFDFRVLTQDRAMRAGLD DVGIGALFGLYDYRYEVCAMLMHSEHLEREYNAGPHTISVPRMRPADGSELSIAPPYPVNDADFMKLVAVLRIAVPYTGM ILSTRESPEMRSALLKCGMSQMSAGSRTDVGAYHKDHTLSTEANLSKLAGQFTLQDERPTNEIVKWLMEEGYVPSWCTAC YRQGRTGEDFMNICKAGDIHDFCHPNSLLTLQEYLMDYADPDLRKKGEQVIAREMGPDASEPLSAQSRKRLERKMKQVLE GEHDVYL

References

[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of hydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.

[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase hydG in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.

[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.

[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme hydG. Biochemistry. 2013;52(48):8696-8707

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K1998010 short</partinfo>
-This part is composed of the HydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of HydE, HydF, and HydG. Within several prokaryotic genomes HydE, HydF, and HydG are found in putative operons with [Fe] hydrogenase structural genes.
-<!-- Add more about the biology of this part here
-===Usage and Biology===
 <!-- -->
@@ Line 17: / Line 11: @@
 <partinfo>BBa_K1998010 parameters</partinfo>
 <!-- -->
+===Overview===
+This part is composed of the <i>hydG</i> gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of <i>hydE, hydF</i>, and <i>hydG</i>. Within several prokaryotic genomes <i>hydE, hydF</i>, and <i>hydG</i> are found in putative operons with [Fe] hydrogenase structural genes.
+<br><br>
+<html><center><img src="https://static.igem.org/mediawiki/parts/b/b5/HydrogenPathwayUpdated2016.jpeg" alt="HydrogenProduction" height="50%"width="75%"></center></html>
+===Biology & Literature===
+<i>hydG</i> is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. <i>hydG</i> breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that <i>hydG</i> cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. <i>hydE</i> and <i>hydF</i> are maturases also required for the assembly of an active hydrogenase [3]. The binding site in <i>hydG</i> can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].
+===Protein information===
+<i>hydG</i><br>
+Mass: 63.74kDa<br>
+Sequence: <br>
+MSVPLQCNAGRLLAGQRPCGVRARLNRRVCVPVTAHGKASATREYAGDFLPGTTISHAWSVERETHHRYRNPAEWINEAA
+IHKALETSKADAQDAGRVREILAKAKEKAFVTEHAPVNAESKSEFVQGLTLEECATLINVDSNNVELMNEIFDTALAIKE
+RIYGNRVVLFAPLYIANHCMNTCTYCAFRSANKGMERSILTDDDLREEVAALQRQGHRRILALTGEHPKYTFDNFLHAVN
+VIASVKTEPEGSIRRINVEIPPLSVSDMRRLKNTDSVGTFVLFQETYHRDTFKVMHPSGPKSDFDFRVLTQDRAMRAGLD
+DVGIGALFGLYDYRYEVCAMLMHSEHLEREYNAGPHTISVPRMRPADGSELSIAPPYPVNDADFMKLVAVLRIAVPYTGM
+ILSTRESPEMRSALLKCGMSQMSAGSRTDVGAYHKDHTLSTEANLSKLAGQFTLQDERPTNEIVKWLMEEGYVPSWCTAC
+YRQGRTGEDFMNICKAGDIHDFCHPNSLLTLQEYLMDYADPDLRKKGEQVIAREMGPDASEPLSAQSRKRLERKMKQVLE
+GEHDVYL
+<br>
+===References===
+[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of <i>hydG</i>, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.
+<br><br>
+[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase <i>hydG</i> in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.
+<br><br>
+[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.
+<br><br>
+[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme <i>hydG</i>. Biochemistry. 2013;52(48):8696-8707