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Field | Value |
---|---|
Namespace | Molecular function |
Short description | Molybdopterin synthase activity |
Full defintion | Catalysis of the conversion of precursor Z to molybdopterin, the final step in molybdopterin biosynthesis. |
Subterm of |
The relationship of GO:0030366 with other GO terms.
Relationship type | GO terms |
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Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0030366, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
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PMID | In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene. J Biol Chem. 1993 Jun 25; 268 (18): 13506–9.PMID: 8514783 The pterin component of the molybdenum cofactor, termed molybdopterin, is synthesized in Escherichia coli by enzymes encoded at the chl loci. A late step in the biosynthetic pathway, the conversion of a molybdopterin intermediate, precursor Z, to molybdopterin, requires the activity of a two-subunit protein, the converting factor. Precursor Z has many of the features of molybdopterin but lacks the dithiolene function essential for molybdenum ligation. Conversion of precursor Z to molybdopterin is accomplished by transfer of sulfur to produce the dithiolene. The present study describes an in vitro system for molybdopterin biosynthesis comprised of purified precursor Z and purified converting factor. It is established that these components are sufficient to yield molybdopterin, identified by conversion to its characteristic products, Form A, Form B, and dicarboxamidomethylmolybdopterin. Under conditions of precursor excess, the formation of molybdopterin was stoichiometric with converting factor, as would be expected in the absence of a sulfur-regenerating system. The labile product of the reaction, molybdopterin, remained associated with the converting factor large subunit. These results establish that the source of sulfur for molybdopterin biosynthesis is the converting factor and suggest that in vivo a novel sulfur cycle must function to resupply sulfur to the converting factor. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | PREDICTED: molybdopterin synthase catalytic subunit-like [Glycine max] gi|356577365|ref|XP_003556797.1| | 4 | ||
– | Molybdopterin synthase catalytic subunit; TAIR: AT2G43760.1 molybdopterin biosynthesis MoaE family protein; Swiss-Prot: sp|O22827|MOC2B_ARATH Molybdopterin synthase catalytic subunit; TrEMBL-Plants: tr|I3S4E4|I3S4E4_LOTJA Molybdopterin synthase catalytic subunit; Found in the gene: LotjaGi6g1v0177300 | 4 | ||
– | Molybdopterin synthase catalytic subunit; TAIR: AT2G43760.1 molybdopterin biosynthesis MoaE family protein; Swiss-Prot: sp|O22827|MOC2B_ARATH Molybdopterin synthase catalytic subunit; TrEMBL-Plants: tr|I3S4E4|I3S4E4_LOTJA Molybdopterin synthase catalytic subunit; Found in the gene: LotjaGi6g1v0177300 | 4 | ||
– | Molybdopterin synthase catalytic subunit; TAIR: AT2G43760.1 molybdopterin biosynthesis MoaE family protein; Swiss-Prot: sp|O22827|MOC2B_ARATH Molybdopterin synthase catalytic subunit; TrEMBL-Plants: tr|I3S4E4|I3S4E4_LOTJA Molybdopterin synthase catalytic subunit; Found in the gene: LotjaGi6g1v0186100 | 4 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Molecular function | Molybdopterin synthase activity | 1 | 25.00 |