ID F8AFR8_PYRYC Unreviewed; 154 AA.
AC F8AFR8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Probable cyclic pyranopterin monophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000256|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224};
GN OrderedLocusNames=PYCH_01100 {ECO:0000313|EMBL:AEH23819.1};
OS Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH23819.1, ECO:0000313|Proteomes:UP000008386};
RN [1] {ECO:0000313|EMBL:AEH23819.1, ECO:0000313|Proteomes:UP000008386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX PubMed=21705594; DOI=10.1128/JB.05345-11;
RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT archaeon Pyrococcus yayanosii CH1.";
RL J. Bacteriol. 193:4297-4298(2011).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01224};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; CP002779; AEH23819.1; -; Genomic_DNA.
DR RefSeq; WP_013904877.1; NC_015680.1.
DR AlphaFoldDB; F8AFR8; -.
DR STRING; 529709.PYCH_01100; -.
DR GeneID; 10836691; -.
DR KEGG; pya:PYCH_01100; -.
DR eggNOG; arCOG01530; Archaea.
DR HOGENOM; CLU_074693_1_2_2; -.
DR OrthoDB; 10067at2157; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000008386; 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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_A; MoaC_A; 1.
DR InterPro; IPR023047; Mo_CF_biosynth-C_arc.
DR InterPro; IPR023045; MoaC.
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 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01224};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01224}.
FT DOMAIN 13..153
FT /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT /evidence="ECO:0000259|Pfam:PF01967"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 109..110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 154 AA; 17255 MW; 338B759C5C85C187 CRC64;
MKLTHVDERG VKMVEVGHKP DVIRKAIAKG RIRLRAETVR LIREGKVEKG NVLAAAQIAA
ILAVKKTPEL IPLCHPIPLT GIDVTFEFGE DYIEVTCEVR AHYKTGVEME ALTGVTVALL
TIWDMVKAVE KDEHGQYPFT RIENIRVVEK MKGE
//
