MOAC_PAENI
ID MOAC_PAENI Reviewed; 169 AA.
AC O31227;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9428706; DOI=10.1111/j.1432-1033.1997.0524a.x;
RA Menendez C., Otto A., Igloi G., Nick P., Brandsch R., Schubach B.,
RA Boettcher B., Brandsch R.;
RT "Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial
RT plasmid: characterization of MoeA as a filament-forming protein with
RT adenosinetriphosphatase activity.";
RL Eur. J. Biochem. 250:524-531(1997).
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; Y10817; CAA71781.1; -; Genomic_DNA.
DR PIR; T44852; T44852.
DR AlphaFoldDB; O31227; -.
DR SMR; O31227; -.
DR UniPathway; UPA00344; -.
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; Plasmid.
FT CHAIN 1..169
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097784"
FT ACT_SITE 133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 81..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 169 AA; 18144 MW; A30E69135FC56BA5 CRC64;
MRLESWSPGL THLRTDGTAH MVDVSEKVES TREATLREQF VQLSEVLLLL TSDGLPKGDA
LAVARISGIL ATKKTSELIP LCHPLPVSQA TVDFVLGSDR VQTLCKAVKT RGVTGVEMEA
LTAVSVAALN LYDMFKAIDK HAVLTDIRVL AKSGGKSGDW DLGTSEEKA
