ID   MOAE_STACT              Reviewed;         150 AA.
AC   Q9ZIM9; B9DLY5;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=Sca_1759;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9675851; DOI=10.1111/j.1574-6968.1998.tb13067.x;
RA   Neubauer H., Pantel I., Goetz F.;
RT   "Characterization of moeB- part of the molybdenum cofactor biosynthesis
RT   gene cluster in Staphylococcus carnosus.";
RL   FEMS Microbiol. Lett. 164:55-62(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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; AF109295; AAC83141.1; -; Genomic_DNA.
DR   EMBL; AM295250; CAL28665.1; -; Genomic_DNA.
DR   RefSeq; WP_015901001.1; NC_012121.1.
DR   AlphaFoldDB; Q9ZIM9; -.
DR   SMR; Q9ZIM9; -.
DR   STRING; 396513.SCA_1759; -.
DR   KEGG; sca:SCA_1759; -.
DR   eggNOG; COG0314; Bacteria.
DR   HOGENOM; CLU_089568_1_2_9; -.
DR   OMA; WPLQRVS; -.
DR   OrthoDB; 1877633at2; -.
DR   BioCyc; SCAR396513:SCA_RS08955-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000444; 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..150
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163103"
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   150 AA;  17276 MW;  81392C264E894927 CRC64;
     MKQFEIVTEP IQTEQHRDFT LNPHQGAVVV FTGHVREWTK GIRTEHLEYE AYIPMAEKKL
     AQIGDEINEQ WPGTIVSIVH RIGPLKISDI AVLIAVSSPH RKDAYAANEY AIDRIKEVVP
     IWKKEIWEDG AEWIGHQRGY HDDAVERGQN