ID   MOEA_STAAR              Reviewed;         419 AA.
AC   Q6GEG1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Molybdopterin molybdenumtransferase;
DE            Short=MPT Mo-transferase;
DE            EC=2.10.1.1;
GN   Name=moeA; OrderedLocusNames=SAR2357;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP. {ECO:0000250}.
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; EC=2.10.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41338.1; -; Genomic_DNA.
DR   RefSeq; WP_000259736.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEG1; -.
DR   SMR; Q6GEG1; -.
DR   KEGG; sar:SAR2357; -.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 651103at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
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; 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   TIGRFAMs; TIGR00177; molyb_syn; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Transferase.
FT   CHAIN           1..419
FT                   /note="Molybdopterin molybdenumtransferase"
FT                   /id="PRO_0000170997"
SQ   SEQUENCE   419 AA;  44976 MW;  65F24ED6DD14BD4F CRC64;
     MVVEKRNPIP VKEAIQRIVN QQSTMPAITV ALEKSLNHIL AEDIVATYDI PRFDKSPYDG
     FAIRSVDSQG ASGQNRIEFK VIDHIGAGSV SDKLVGDHEA VRIMTGAQIP NGADAVVMFE
     QTIELEDTFT IRKPFSKNEN ISLKGEETTT GDVVLKKGQV INPGAIAVLA TYGYAEVKVI
     KQPSVAVIAT GSELLDVNDV LEDGKIRNSN GPMIRALAEK LGLEVGIYKT QQDDLDSGIQ
     VVKEAMEKHD IVITTGGVSV GDFDYLPEIY KAVKAEVLFN KVAMRPGSVT TVAFADGKYL
     FGLSGNPSAC FTGFELFVKP AVKHMCGALE VFPQIIKATL MEDFTKANPF TRFIRAKATL
     TSAGATVVPS GFNKSGAVVA IAHANCMVML PGGSRGFKAG HTVDIILTES DAAEEELLL