ID S4WBA9_9BACT Unreviewed; 313 AA.
AC S4WBA9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575, 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};
OS uncultured bacterium FPPP_13C3.
OC Bacteria; environmental samples.
OX NCBI_TaxID=1343845 {ECO:0000313|EMBL:AGO87978.1};
RN [1] {ECO:0000313|EMBL:AGO87978.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24030600; DOI=10.1038/ismej.2013.152;
RA Wright J.J., Mewis K., Hanson N.W., Konwar K.M., Maas K.R., Hallam S.J.;
RT "Genomic properties of Marine Group A bacteria indicate a role in the
RT marine sulfur cycle.";
RL ISME J. 8:455-468(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|ARBA:ARBA00001637,
CC 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; KF170421; AGO87978.1; -; Genomic_DNA.
DR AlphaFoldDB; S4WBA9; -.
DR UniPathway; UPA00344; -.
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; cd01420; MoaC_PE; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR012247; MoaC_MogA.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00581; moaC; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF036594; MoaC_MogA; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01224};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01224}.
FT DOMAIN 161..304
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT ACT_SITE 126
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 111..112
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 313 AA; 33731 MW; AADC034ABC52599F CRC64;
MEELSHLDEE GNVKMVDVTN KTSNNRIAKA EGKITMLPET IIAIRSSSLP KGNVLTTAKI
AGILAAKKTS DLIPMCHQLN LSNIDIVFKI ESKAITISSE VKVKESTGVE MEALTAVSIT
ALTIYDMCKA IDKSMSISEI KLIEKVGGKT DHLTDYRPSI GVITISDSIS KSEAKDISGL
ILADGFKEVG CNVDHQCILP DGSKELLSTI KLWSSEGVEL IITTGGTGLG PRDLTIETLE
KHFNSNLPGI EQALHAYGRS KVKTSILSRL KAGLIDKTIV ICIPGSPSAA KDALNVLIPT
IFHLFHMMKG EKH
//
