ID   MOAC_SHISS              Reviewed;         161 AA.
AC   Q3Z401;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN   Name=moaC {ECO:0000255|HAMAP-Rule:MF_01224}; OrderedLocusNames=SSON_0762;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC       (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC         pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC         EC=4.6.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01224};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; CP000038; AAZ87511.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z401; -.
DR   SMR; Q3Z401; -.
DR   EnsemblBacteria; AAZ87511; AAZ87511; SSON_0762.
DR   KEGG; ssn:SSON_0762; -.
DR   HOGENOM; CLU_074693_1_1_6; -.
DR   OMA; IWDMVKS; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01420; MoaC_PE; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; Mo_CF_biosynth-C.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
DR   TIGRFAMs; TIGR00581; moaC; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis.
FT   CHAIN           1..161
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_1000054146"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         113..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   161 AA;  17495 MW;  A2251D25E4540A4D CRC64;
     MSQLTHINAA GEAHMVDVSA KAETVREARA EAFVTMRSET LAMIIDGRHH KGDVFATARI
     VGIQAAKRTW DLIPLCHPLM LSKVEVNLQA EPEHNRVRIE TLCRLTGKTG VEMEALTAAS
     VAALTIYDMC KAVQKDMVIG PVRLLAKSGG KSGDFKVEAD D