ID A0A016RRT2_9BILA Unreviewed; 393 AA. AC A0A016RRT2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 13-FEB-2019, entry version 12. DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090}; DE EC=2.10.1.1 {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 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}; GN Name=Acey_s0393.g609 {ECO:0000313|EMBL:EYB81080.1}; GN ORFNames=Y032_0393g609 {ECO:0000313|EMBL:EYB81080.1}; OS Ancylostoma ceylanicum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; OC Ancylostomatinae; Ancylostoma. OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB81080.1, ECO:0000313|Proteomes:UP000024635}; RN [1] {ECO:0000313|Proteomes:UP000024635} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635}; RX PubMed=25730766; DOI=10.1038/ng.3237; RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W., RA Aroian R.V.; RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma RT ceylanicum identify infection-specific gene families."; RL Nat. Genet. 47:416-422(2015). CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the CC molybdenum cofactor. In the first step, molybdopterin is CC adenylated. Subsequently, molybdate is inserted into adenylated CC molybdopterin and AMP is released. CC {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 + CC Mo-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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYB81080.1}. 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; JARK01001729; EYB81080.1; -; Genomic_DNA. DR UniPathway; UPA00344; -. DR Proteomes; UP000024635; Unassembled WGS sequence. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:InterPro. DR CDD; cd00887; MoeA; 1. DR Gene3D; 2.40.340.10; -; 1. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR036425; MoaB/Mog-like_dom_sf. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR InterPro; IPR038987; MoeA-like. DR InterPro; IPR005111; MoeA_C_domain_IV. DR InterPro; IPR036688; MoeA_C_domain_IV_sf. DR InterPro; IPR005110; MoeA_linker/N. DR InterPro; IPR036135; MoeA_linker/N_sf. DR PANTHER; PTHR10192; PTHR10192; 1. DR Pfam; PF00994; MoCF_biosynth; 1. DR Pfam; PF03454; MoeA_C; 1. DR Pfam; PF03453; MoeA_N; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR SUPFAM; SSF63867; SSF63867; 1. DR SUPFAM; SSF63882; SSF63882; 1. DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024635}; 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|RuleBase:RU365090}; KW Reference proteome {ECO:0000313|Proteomes:UP000024635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|RuleBase:RU365090}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 393 Molybdopterin molybdenumtransferase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001488447. FT DOMAIN 160 304 MoCF_biosynth. {ECO:0000259|SMART: FT SM00852}. SQ SEQUENCE 393 AA; 42150 MW; E8B1DA8B0386EDDF CRC64; MLYLLNIFLT IGQVLAERVV AKEDVPEVRT SIKDGYAVLA SDPPGERRVI GSSTAGAPFL GTISAGECVR VSTGAFVPDG ADAVAMVENT RLVKHDGIEE LIISVDTTVK PGQDIRMPGS DIRKGDLLLD SGCVLGSAEI GILAGSGKRS VLMYRKPKVC VLSTGNELVE CTADEVPPGH IRDTNRPQLI ALFGSLGFKA IDAGIAADRR ECLVEAIRVS FQYAHVLVTS GGVSMGEKDL LKDVLMKDFG FEIHFGRVWM KPGLPTTFAT GHMFGDKKFV FALPGNPVSS WVTAQLFAVP LLRKAAGHTR LFQQEIKVQL AEDINLDSRP EYRRAWLQHG GAIPTAITTG NQISSRLMSL SGANVLLKVP GKSAECTRLP AGEIVDALWL GAM //