MOAC_SULAC
ID MOAC_SULAC Reviewed; 143 AA.
AC Q4JAB2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Saci_0905;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80268.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JAB2; -.
DR SMR; Q4JAB2; -.
DR STRING; 330779.Saci_0905; -.
DR PRIDE; Q4JAB2; -.
DR EnsemblBacteria; AAY80268; AAY80268; Saci_0905.
DR KEGG; sai:Saci_0905; -.
DR PATRIC; fig|330779.12.peg.865; -.
DR eggNOG; arCOG01530; Archaea.
DR HOGENOM; CLU_074693_1_2_2; -.
DR OMA; IWDMVKS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001018; 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..143
FT /note="Probable cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097863"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 143 AA; 16040 MW; E632266FDA2870F9 CRC64;
MIDISGKDIV LREAIAEGFI KLKKDTIEKI TKREIEKGDV IATAKVAGIL AAKKTHELLP
MCHPIPLEYI NVEIEIENDG LKVVSTVRAH YRTGVEMEAL TATSIALLTI WDMVKKYEKD
EEGQYPLTEI SKIRVVSKIK SYG
