ID A0A0G2JBQ6_9EURO Unreviewed; 527 AA.
AC A0A0G2JBQ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=molybdopterin adenylyltransferase {ECO:0000256|ARBA:ARBA00012509};
DE EC=2.7.7.75 {ECO:0000256|ARBA:ARBA00012509};
GN ORFNames=EMCG_06425 {ECO:0000313|EMBL:KKZ67896.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ67896.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(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|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 -!- 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:KKZ67896.1}.
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DR EMBL; LCZI01000179; KKZ67896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2JBQ6; -.
DR VEuPathDB; FungiDB:EMCG_06425; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000034164; 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 CDD; cd00887; MoeA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 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 Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 212..400
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 527 AA; 56344 MW; 2AB29569F30B615D CRC64;
MAISYEGAIC IIKAEATASS HTFQESTETI QLYKALNRIS KSTHLSPLST PKWDTSAMDG
YALSSKATQW ASEQNPVAFA VKATIAAGDE PPAISGAPEN GIYPCVEIMT GARFPPTVGG
ELPFDCCVRV EDTVLATASS ITKGSSTREK AGNFIHVGKP ARPNQHKRLA GEDFERGDMI
IEGGSIIRPP HVMALASVGI ETLTVLRKPR VAVFSTGSEL IKAGDKSPPK FSSTTASGGI
PDVNGPYISA TLEEQGCDVD FLEVIEDNSE IAAKKVISHL QQGRWQYDML ITTGGVSVGK
FDFIREAMER LNASILFHRV AMRPGHPALF ATIPYTSGSW ASGSCNGNVT GTPILPPFTS
PSEHVNNKKE EKNVAFFGLP GNPIASAACL QFLVMPFLRT LVSKPCDLPI PAIVRPLEKY
HQHANGDKKN GVRQGDRAGG LDLASGISTN RKVVASFPSD KDVFRAGKVL SKGGHGIMEV
SITTDHSPGK VSPFLGADCW VHVHQGCAEL REGDYVDLYP LMSGRAI
//
