GO_REF:0000120

Combined automated GO annotation using multiple IEA methods

file:PSEPK/moaC/moaC-uniprot.txt

UniProtKB reviewed entry for moaC

UniProt (HAMAP MF_01224) assigns Q88NC0 the MoaC cPMP synthase reaction in molybdopterin biosynthesis.

"FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP)."

file:interpro/panther/PTHR22960/PTHR22960-entries.csv

PANTHER representative entries for moaC

The local PANTHER export places Q88NC0 in the MoaC-specific PTHR22960:SF29 subfamily.

"Q88NC0,Cyclic pyranopterin monophosphate synthase,protein,160488,Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440),Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440),moaC,156,PTHR22960:SF29,CYCLIC PYRANOPTERIN MONOPHOSPHATE SYNTHASE,True"

PMID:25941396

Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis.

file:PSEPK/moaC/moaC-deep-research-falcon.md

Falcon deep research on moaC (Edison Scientific Literature)

"MoaC** is the **cPMP synthase** that converts **3′,8-cH2GTP → cPMP** via a complex rearrangement that constructs the pyranopterin framework and cyclic phosphate."
"bacterial MoaC is treated in the literature as a **soluble intracellular/cytosolic biosynthetic enzyme** functioning in early Moco biosynthesis rather than a membrane or secreted protein"
"MoaC **forms a hexamer composed of a trimer of dimers**; the **active site lies at the interface of each dimer**"

file:PSEPK/moaC/moaC-deep-research-openscientist.md

OpenScientist gene research for moaC

The report states the same MoaC reaction recorded in the target UniProt entry.

"| Catalytic reaction (UniProt) | 3′,8-cH₂GTP = cyclic pyranopterin phosphate + diphosphate |"
The report incorrectly identifies PP_3457 as mogA rather than mobA.

"(PP_2123, Mo insertase) and *mogA* (PP_3457) — i.e., every step needed to convert GTP into mature Moco (KEGG module M00880)."
The report presents unsaved target-alignment and catalytic-residue analysis.

"**Quantitative homology evidence (this work):** A pairwise alignment of Q88NC0 against the experimentally and structurally characterized *E. coli* MoaC (P0A738) shows **72.7% amino-acid identity** (112/154 aligned positions), and the catalytically essential *E. coli* **Asp128 aligns with an aspartate in the P. putida sequence**."
The report acknowledges the absence of direct KT2440 MoaC characterization.

"- **Organism-specific data:** Direct biochemical/genetic characterization of MoaC has been done in *E. coli*, *T. thermophilus*, *M. tuberculosis* and human MOCS1B, **not specifically in *P. putida* KT2440**."