TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry P30748 (MOAD_ECOLI)
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E. coli MoaD forms the 2:2 MoaD-MoaE synthase and a 2:2 MoeB-MoaD activation complex (experimental, PubMed-tied).
"Forms a stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation of MoaD by MoeB."
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
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In Escherichia coli, MoeB adenylates the MoaD C terminus within a MoeB-MoaD complex, and the thiocarboxylated MoaD is the sulfur donor for Moco biosynthesis.
"a sulphurtransferase converts the MoaD acyl-adenylate to a thiocarboxylate that acts as the sulphur donor during Moco biosynthesis"
Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold.
PANTHER representative entries for the molybdopterin synthase sulfur-carrier family
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PTHR33359:SF1 contains the Escherichia coli MoaD ortholog used for the ISS complex proposal.
"P30748,Molybdopterin synthase sulfur carrier subunit,protein,83333,Escherichia coli (strain K12),Escherichia coli (strain K12),moaD,81,PTHR33359:SF1,MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT,True"
OpenScientist gene research for moaD
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The report reviews MoaD activation and sulfur donation in molybdopterin synthesis.
"The gene **moaD** (UniProt **Q88NB9**; ordered locus **PP_1293**) of *Pseudomonas putida* strain KT2440 encodes the **small sulfur-carrier subunit of molybdopterin (MPT) synthase**, the enzyme that catalyzes the **second of the four conserved steps of molybdenum cofactor (Moco) biosynthesis**."