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 27-MAR-2024, entry version 98.
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; Bacillota; 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; 93061.SAOUHSC_02543; -.
DR PaxDb; 1280-SAXN108_2523; -.
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 OrthoDB; 9794429at2; -.
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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00581; moaC; 1.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, 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
//
