MOAE_STAAR
ID MOAE_STAAR Reviewed; 148 AA.
AC Q6GEG3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Molybdopterin synthase catalytic subunit;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E;
DE AltName: Full=Molybdopterin-converting factor large subunit;
DE AltName: Full=Molybdopterin-converting factor subunit 2;
GN Name=moaE; OrderedLocusNames=SAR2355;
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: Converts molybdopterin precursor Z into molybdopterin. This
CC requires the incorporation of two sulfur atoms into precursor Z to
CC generate a dithiolene group. The sulfur is provided by MoaD (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12;
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also
CC stable as homodimer. The enzyme changes between these two forms during
CC catalysis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
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DR EMBL; BX571856; CAG41336.1; -; Genomic_DNA.
DR RefSeq; WP_000808500.1; NC_002952.2.
DR AlphaFoldDB; Q6GEG3; -.
DR SMR; Q6GEG3; -.
DR KEGG; sar:SAR2355; -.
DR HOGENOM; CLU_089568_1_2_9; -.
DR OMA; WPLQRVS; -.
DR OrthoDB; 1877633at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Transferase.
FT CHAIN 1..148
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163100"
FT BINDING 34..36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 148 AA; 17339 MW; B4292F340523EA19 CRC64;
MKQFEIVTEP IQTEQYREFT INEYQGAVVV FTGHVREWTK GVKTEYLEYE AYIPMAEKKL
AQIGDEINEK WPGTITSIVH RIGPLQISDI AVLIAVSSPH RKDAYRANEY AIERIKEIVP
IWKKEIWEDG SKWQGHQKGN YEEAKREE