MOAC_PYRFU
ID MOAC_PYRFU Reviewed; 156 AA.
AC Q8TZX1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable 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=PF1854;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81978.1; -; Genomic_DNA.
DR RefSeq; WP_011012994.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZX1; -.
DR SMR; Q8TZX1; -.
DR STRING; 186497.PF1854; -.
DR PRIDE; Q8TZX1; -.
DR EnsemblBacteria; AAL81978; AAL81978; PF1854.
DR GeneID; 41713674; -.
DR KEGG; pfu:PF1854; -.
DR PATRIC; fig|186497.12.peg.1925; -.
DR eggNOG; arCOG01530; Archaea.
DR HOGENOM; CLU_074693_1_2_2; -.
DR OMA; IWDMVKS; -.
DR OrthoDB; 104538at2157; -.
DR PhylomeDB; Q8TZX1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001013; 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; cd01419; MoaC_A; 1.
DR Gene3D; 3.30.70.640; -; 1.
DR HAMAP; MF_01224_A; MoaC_A; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR023047; Mo_CF_biosynth-C_arc.
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; Reference proteome.
FT CHAIN 1..156
FT /note="Probable cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097860"
FT ACT_SITE 124
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 109..110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 156 AA; 17600 MW; 5C7CE3F354F6CE10 CRC64;
MKLTHVDEKG VKMVEVGHKK DMYRRAIAKG RIKLKPETIK LIREGKIEKG NVLAAAQIAG
ILAVKKTFDI IPLCHPIPLT GVDITFDFGE DYIEVTCEVR AIYKTGVEME ALTGVSVALL
TIWDMVKAVE KDEKGQYPYT KIEEIRVVEK IKEERS
