ID MOAA_METTM Reviewed; 87 AA. AC Q50746; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-JUL-2008, entry version 43. DE RecName: Full=Probable molybdenum cofactor biosynthesis protein A; DE Flags: Fragment; GN Name=moaA; OS Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96163477; PubMed=8575452; RA Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.; RT "The tungsten formylmethanofuran dehydrogenase from Methanobacterium RT thermoautotrophicum contains sequence motifs characteristic for RT enzymes containing molybdopterin dinucleotide."; RL Eur. J. Biochem. 234:910-920(1995). CC -!- FUNCTION: Together with moaC, is involved in the conversion of a CC guanosine derivative (5'-GTP) into molybdopterin precursor Z (By CC similarity). CC -!- COFACTOR: Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and CC the GTP-derived substrate (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X87968; CAA61207.1; -; Genomic_DNA. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01225; -; 1. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S_bd_CS. DR InterPro; IPR007197; Radical_SAM. DR Pfam; PF04055; Radical_SAM; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 3: Inferred from homology; KW 4Fe-4S; GTP-binding; Iron; Iron-sulfur; Metal-binding; KW Molybdenum cofactor biosynthesis; Nucleotide-binding; KW S-adenosyl-L-methionine. FT CHAIN 1 >87 Probable molybdenum cofactor biosynthesis FT protein A. FT /FTId=PRO_0000153021. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 26 26 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 29 29 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT BINDING 15 15 GTP (By similarity). FT BINDING 28 28 S-adenosyl-L-methionine (By similarity). FT BINDING 62 62 GTP (By similarity). FT BINDING 66 66 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT NON_TER 87 87 SQ SEQUENCE 87 AA; 9874 MW; A97432C6E439F909 CRC64; MQVHDNHRRP LVSLRISVTG RCNVSCIYCH RDGILRSDEE MSPEDIENIC RVASDLGVKK IRLSGGEPLI RDDIVEIVEK INSIGFR //