ID M0M8R6_HALMO Unreviewed; 166 AA.
AC M0M8R6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=C448_11366 {ECO:0000313|EMBL:EMA42126.1};
OS Halococcus morrhuae DSM 1307.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA42126.1, ECO:0000313|Proteomes:UP000011568};
RN [1] {ECO:0000313|EMBL:EMA42126.1, ECO:0000313|Proteomes:UP000011568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA42126.1,
RC ECO:0000313|Proteomes:UP000011568};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA42126.1}.
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DR EMBL; AOMC01000135; EMA42126.1; -; Genomic_DNA.
DR RefSeq; WP_004054876.1; NZ_AOMC01000135.1.
DR AlphaFoldDB; M0M8R6; -.
DR STRING; 931277.C448_11366; -.
DR PATRIC; fig|931277.6.peg.2222; -.
DR eggNOG; arCOG01530; Archaea.
DR OrthoDB; 10067at2157; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000011568; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011568}.
FT DOMAIN 22..161
FT /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT /evidence="ECO:0000259|Pfam:PF01967"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 82..84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 166 AA; 17789 MW; 34CF103FDB271259 CRC64;
MSDDPGDASD LTHTTTEGDA QMVDVGAKPD SARRAVARGT IHLRESTVAA VADDGIEKGN
VLATARIGAI RAVKHTWETI PLCHQIPITN VETEFTLDDD HVTLTVTVET TGKTGCEMEA
LQGVTTGLNT VWDMTKAAEK DEDGQYPATA IEGVRVLEKE KTLDEN
//
