ID D9UTM4_STRS3 Unreviewed; 402 AA.
AC D9UTM4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
GN ORFNames=SSLG_02590 {ECO:0000313|EMBL:EFL00532.1};
OS Streptomyces sp. (strain SPB78).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL00532.1, ECO:0000313|Proteomes:UP000005781};
RN [1] {ECO:0000313|EMBL:EFL00532.1, ECO:0000313|Proteomes:UP000005781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB78 {ECO:0000313|EMBL:EFL00532.1,
RC ECO:0000313|Proteomes:UP000005781};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain SPB78.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657742; EFL00532.1; -; Genomic_DNA.
DR AlphaFoldDB; D9UTM4; -.
DR STRING; 591157.SSLG_02590; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_063423_1_0_11; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000005781; 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; 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; 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 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 223..365
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 149..150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 402 AA; 40509 MW; BB81A72E60328AC8 CRC64;
MSARHRPARD AREPITGALR LMTATPAGAA APEPADPPSG GLTHLDSSGA ARMVDVTRKD
VTARTARATG RVLVTPEVVA LLRGEGLPKG DALATARIAG IMGAKRTPDL VPLCHPLALS
GVTVDLEVTD EAVAITATVR TTDRTGVEME ALTAVSVAAL TVVDMVKAVD KAATITDIRV
ETKTGGKSGD WHREGQSAGT GEAARGRPRE AAPRTPLGAR TALVVTASNR AAAGVYPDRG
GPLIAEALRA WGFATEGPQV VPDGAPVEAA LRAAIETGYG VVVTTGGTGL TPTDLTPEAT
RALLDREIPG VAEAIRAEGL GKVPSAALSR GLAGVAGTTL VVNLPGSTGG VRDGLAVLER
WLPHAVDQIH GGDHRPAPGQ TGAGTHPGPG TSGPAENAGS PS
//
