ID Q571C2_MOUSE Unreviewed; 141 AA. AC Q571C2; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 22-FEB-2023, entry version 75. DE RecName: Full=Gephyrin {ECO:0000256|RuleBase:RU365090}; DE Includes: DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090}; DE Short=MPT Mo-transferase {ECO:0000256|RuleBase:RU365090}; DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090}; DE AltName: Full=Domain E {ECO:0000256|RuleBase:RU365090}; DE Includes: DE RecName: Full=Molybdopterin adenylyltransferase {ECO:0000256|RuleBase:RU365090}; DE Short=MPT adenylyltransferase {ECO:0000256|RuleBase:RU365090}; DE EC=2.7.7.75 {ECO:0000256|RuleBase:RU365090}; DE AltName: Full=Domain G {ECO:0000256|RuleBase:RU365090}; DE Flags: Fragment; GN Name=Gphn {ECO:0000313|MGI:MGI:109602}; GN Synonyms=mKIAA1385 {ECO:0000313|EMBL:BAD90192.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAD90192.1}; RN [1] {ECO:0000313|EMBL:BAD90192.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adult pancreatic islet {ECO:0000313|EMBL:BAD90192.1}; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene. The RT Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs Identified by RT Screening of Terminal sequences of cDNA Clones Randomly Sampled from Size- RT Fractionated Libraries.."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum CC cofactor. In the first step, molybdopterin is adenylated. Subsequently, CC molybdate is inserted into adenylated molybdopterin and AMP is CC released. {ECO:0000256|RuleBase:RU365090}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin + CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698, CC ChEBI:CHEBI:62727; Evidence={ECO:0000256|RuleBase:RU365090}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo- CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727, CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; CC Evidence={ECO:0000256|RuleBase:RU365090}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU365090}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000256|RuleBase:RU365090}. CC -!- SIMILARITY: Belongs to the MoeA family. CC {ECO:0000256|RuleBase:RU365090}. 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; AK220267; BAD90192.1; -; mRNA. DR AlphaFoldDB; Q571C2; -. DR PeptideAtlas; Q571C2; -. DR AGR; MGI:109602; -. DR MGI; MGI:109602; Gphn. DR UniPathway; UPA00344; -. DR ChiTaRS; Gphn; mouse. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1. DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1. DR InterPro; IPR036425; MoaB/Mog-like_dom_sf. DR InterPro; IPR038987; MoeA-like. DR InterPro; IPR005111; MoeA_C_domain_IV. DR InterPro; IPR036688; MoeA_C_domain_IV_sf. DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1. DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1. DR Pfam; PF03454; MoeA_C; 1. DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1. DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1. PE 2: Evidence at transcript level; KW Magnesium {ECO:0000256|RuleBase:RU365090}; KW Metal-binding {ECO:0000256|RuleBase:RU365090}; KW Molybdenum {ECO:0000256|RuleBase:RU365090}; KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150, KW ECO:0000256|RuleBase:RU365090}; KW Transferase {ECO:0000256|RuleBase:RU365090}. FT DOMAIN 63..137 FT /note="MoeA C-terminal" FT /evidence="ECO:0000259|Pfam:PF03454" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD90192.1" SQ SEQUENCE 141 AA; 15827 MW; 3BBE81039D6DBB00 CRC64; FGRVFMKPGL PTTFATLDID GVRKIIFALP GNPVSAVVTC NLFVVPALRK MHGILDPRPT IIKARLSCDV KLDPRPEYHR CILTWHHQEP LPWAQSTGNQ MSSRLMSMRS ANGLLMLPPK TEQYVELHKG EVVDVMVIGR L //