ID   MOAE_RALSO              Reviewed;         176 AA.
AC   Q8XZR3;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=RSc1332; ORFNames=RS02854;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646052; CAD15034.1; -; Genomic_DNA.
DR   RefSeq; WP_011001281.1; NC_003295.1.
DR   AlphaFoldDB; Q8XZR3; -.
DR   SMR; Q8XZR3; -.
DR   STRING; 267608.RSc1332; -.
DR   EnsemblBacteria; CAD15034; CAD15034; RSc1332.
DR   GeneID; 60500854; -.
DR   KEGG; rso:RSc1332; -.
DR   eggNOG; COG0314; Bacteria.
DR   HOGENOM; CLU_089568_2_1_4; -.
DR   OMA; GEICLFV; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001436; 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; Reference proteome; Transferase.
FT   CHAIN           1..176
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163091"
FT   BINDING         36..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   176 AA;  19151 MW;  059A00CA3AE33C23 CRC64;
     MPTIRVQEAD FDLGAEIAAL RAGRPQIGAV ASFIGTVRDI NDGSGVSEME LEHYPGMTEK
     ALANIVDAAM QRWDLIDALV IHRVGKLRPE DQIVLVAVAS GHRGEAFAAC EFIMDYLKSE
     APFWKKEQTA QGARWVDARV TDERALARWG IVTDNASAAT AQAASANDQN QKDRDA