MOAC_AQUAE
ID MOAC_AQUAE Reviewed; 254 AA.
AC O66810;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000250|UniProtKB:P0A738};
DE EC=4.6.1.17 {ECO:0000250|UniProtKB:P0A738};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000250|UniProtKB:P0A738};
GN Name=moaC; OrderedLocusNames=aq_527;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000250|UniProtKB:P0A738}.
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:0000250|UniProtKB:P0A738};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000250|UniProtKB:P0A738}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250|UniProtKB:P0A738}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaC family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06772.1; -; Genomic_DNA.
DR PIR; F70347; F70347.
DR RefSeq; NP_213370.1; NC_000918.1.
DR RefSeq; WP_010880308.1; NC_000918.1.
DR AlphaFoldDB; O66810; -.
DR SMR; O66810; -.
DR STRING; 224324.aq_527; -.
DR EnsemblBacteria; AAC06772; AAC06772; aq_527.
DR KEGG; aae:aq_527; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_063423_1_1_0; -.
DR InParanoid; O66810; -.
DR OrthoDB; 1877633at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR Gene3D; 3.30.70.640; -; 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; Reference proteome.
FT CHAIN 1..254
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097783"
FT REGION 1..143
FT /note="Molybdenum cofactor biosynthesis protein C"
FT REGION 144..254
FT /note="Unknown"
FT ACT_SITE 114
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 63..65
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
SQ SEQUENCE 254 AA; 28737 MW; 763F0BDA8B37F186 CRC64;
MRTVDITTKI ETLREAKAYG RIRLKPETVK LIKENKVPKG NLVEATKLSG IFGAKKTGEL
LPFCHPIPLD FVALEVKVNE DNLEVFSTVR GIARTGYEME ALTAVTTALL NVYDMCKALD
DSMVIEEVKL LEKSGGKSDW FRRLDGVKVN LHAENEGLRK IAEDYLKELG ATFAEEAELY
ISIGDNLPIN KEIRSLERVI SLYDFRRNPK EVGKEIRVGW SDDALIIILP ESEEKIRFFF
ETFGGIIGNL LCRR
