ID   MOAC_STAA8              Reviewed;         164 AA.
AC   Q2FVX9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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, ECO:0000269|PubMed:23627491};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN   Name=moaC {ECO:0000255|HAMAP-Rule:MF_01224};
GN   OrderedLocusNames=SAOUHSC_02543;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23627491; DOI=10.1021/ja401781t;
RA   Hover B.M., Loksztejn A., Ribeiro A.A., Yokoyama K.;
RT   "Identification of a cyclic nucleotide as a cryptic intermediate in
RT   molybdenum cofactor biosynthesis.";
RL   J. Am. Chem. Soc. 135:7019-7032(2013).
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, ECO:0000269|PubMed:23627491}.
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         ECO:0000269|PubMed:23627491};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.06 uM for (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
CC         {ECO:0000269|PubMed:23627491};
CC         Note=kcat is 0.17 min(-1). {ECO:0000269|PubMed:23627491};
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; CP000253; ABD31557.1; -; Genomic_DNA.
DR   RefSeq; WP_000134528.1; NZ_LS483365.1.
DR   RefSeq; YP_501006.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVX9; -.
DR   SMR; Q2FVX9; -.
DR   STRING; 1280.SAXN108_2523; -.
DR   EnsemblBacteria; ABD31557; ABD31557; SAOUHSC_02543.
DR   GeneID; 3921132; -.
DR   KEGG; sao:SAOUHSC_02543; -.
DR   PATRIC; fig|93061.5.peg.2293; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_9; -.
DR   OMA; IWDMVKS; -.
DR   UniPathway; UPA00344; -.
DR   PRO; PR:Q2FVX9; -.
DR   Proteomes; UP000008816; 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   1: Evidence at protein level;
KW   Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..164
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_1000054151"
FT   ACT_SITE        131
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         116..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   164 AA;  17694 MW;  7DEC5FEFD9A55E62 CRC64;
     MTEFTHINQQ GHAKMVDVSD KQITKRTAVA HSSITVNETI FKQISNNTNT KGNVLNTAQI
     AGIMAAKNTS TLIPMCHPLP LTGIDVHFSW DETNAPLYTL NIQTTVSTTG KTGVEMEALT
     AASATALTIY DMTKAVDKGM IIGETYLESK SGGKSGDFQR QSNQ