ID A0A016RRT2_9BILA Unreviewed; 393 AA. AC A0A016RRT2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-OCT-2022, entry version 20. DE RecName: Full=MoCF_biosynth domain-containing protein {ECO:0000259|SMART:SM00852}; GN Name=Acey_s0393.g609 {ECO:0000313|EMBL:EYB81080.1}; GN Synonyms=Acey-moc-1 {ECO:0000313|EMBL:EYB81080.1}; GN ORFNames=Y032_0393g609 {ECO:0000313|EMBL:EYB81080.1}; OS Ancylostoma ceylanicum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida; OC Ancylostomatoidea; Ancylostomatidae; 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 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|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}. CC -!- SIMILARITY: Belongs to the MoeA family. CC {ECO:0000256|RuleBase:RU365090}. CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family. CC {ECO:0000256|ARBA:ARBA00008339}. CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family. CC {ECO:0000256|ARBA:ARBA00007589}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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: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 GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule. 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 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 Reference proteome {ECO:0000313|Proteomes:UP000024635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|RuleBase:RU365090}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..393 FT /note="MoCF_biosynth domain-containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5001488447" FT DOMAIN 160..304 FT /note="MoCF_biosynth" FT /evidence="ECO:0000259|SMART: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 //