MOEA_STAAW
ID MOEA_STAAW Reviewed; 419 AA.
AC Q8NVA1;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1;
GN Name=moeA; OrderedLocusNames=MW2191;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB96056.1; -; Genomic_DNA.
DR RefSeq; WP_000259724.1; NC_003923.1.
DR AlphaFoldDB; Q8NVA1; -.
DR SMR; Q8NVA1; -.
DR EnsemblBacteria; BAB96056; BAB96056; BAB96056.
DR KEGG; sam:MW2191; -.
DR HOGENOM; CLU_010186_7_1_9; -.
DR OMA; MTGAMVP; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000418; 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_0000170999"
SQ SEQUENCE 419 AA; 44990 MW; 1304751BC56A94F1 CRC64;
MVVEKRNPIP VKEAIQRIVN QQSSMPAITV ALEKSLNHIL AEDIVATYDI PRFDKSPYDG
FAIRSVDSQG ASGQNRIEFK VIDHIGAGSV SDKLVGDHEA VRIMTGAQIP NGADAVVMFE
QTIELEDTFT IRKPFSKNEN ISLKGEETTT GDVVLKKGQV INPGAIAVLA TYGYAEVKVI
KQPSVAVIAT GSELLDVNDV LEDGKIRNSN GPMIRALAEK LGLEVGIYKT QKDDLDSGIQ
VVKEAMEKHD IVITTGGVSV GDFDYLPEIY KAVKAEVLFN KVAMRPGSVT TVAFVDGKYL
FGLSGNPSAC FTGFELFVKP AVKHMCGALE VFPQIIKATL MEDFTKANPF TRFIRAKATL
TSAGATVVPS GFNKSGAVVA IAHANCMVML PGGSRGFKAG HTVDIILTES DAAEEELLL