MOEA_STAAC
ID MOEA_STAAC Reviewed; 419 AA.
AC Q5HDT4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1;
GN Name=moeA; OrderedLocusNames=SACOL2266;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38486.1; -; Genomic_DNA.
DR RefSeq; WP_000259718.1; NC_002951.2.
DR AlphaFoldDB; Q5HDT4; -.
DR SMR; Q5HDT4; -.
DR EnsemblBacteria; AAW38486; AAW38486; SACOL2266.
DR KEGG; sac:SACOL2266; -.
DR HOGENOM; CLU_010186_7_1_9; -.
DR OMA; MTGAMVP; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000530; 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_0000170994"
SQ SEQUENCE 419 AA; 45017 MW; 98947D86FA6A92A3 CRC64;
MVVEKRNPIP VKEAIQRIVN QQSSMPAITV ALEKSLNHIL AEDIVATYDI PRFDKSPYDG
FAIRSVDSQG ASGQNRIEFK VIDHIGAGSV SDKLVGDHEA VRIMTGAQIP NGADAVVMFE
QTIELEDTFT IRKPFSKNEN ISLKGEETKT 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