ID F0S3P2_DESTD Unreviewed; 303 AA.
AC F0S3P2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575};
GN OrderedLocusNames=Dester_0823 {ECO:0000313|EMBL:ADY73464.1};
OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73464.1, ECO:0000313|Proteomes:UP000007102};
RN [1] {ECO:0000313|EMBL:ADY73464.1, ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX PubMed=22675590; DOI=10.4056/sigs.2465574;
RA Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfur-reducer
RT Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT hydrothermal vent.";
RL Stand. Genomic Sci. 5:407-415(2011).
RN [2] {ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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DR EMBL; CP002543; ADY73464.1; -; Genomic_DNA.
DR RefSeq; WP_013638418.1; NC_015185.1.
DR AlphaFoldDB; F0S3P2; -.
DR STRING; 868864.Dester_0823; -.
DR KEGG; dte:Dester_0823; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_063423_1_1_0; -.
DR InParanoid; F0S3P2; -.
DR OMA; TIYKTGV; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000007102; 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 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 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 MOLYBDENUMTRANSFERASE; 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 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000007102}.
FT DOMAIN 150..294
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 303 AA; 33196 MW; F341789C1EEE046A CRC64;
MKTIDITTKF DTLRTAKAVG RIKLSPETVK KILNKEIPKG DVLSTAQIAG IMGAKKTAEL
IPFCHPIPID HIELKTKVGE DFIEVEAEVK GIWRTGYEVE AMNAVMMALL NIFDMCKGFD
KNMVIEGVKI IFKSGGKSDW GEDLSGLKAA VITVSDSAYA GKREDRSGLL AKEILEQFRA
EVVGYTIVPD EKEAIKEAIK KFKQMEVNLI VTTGGTGFSK RDVTPEATSE VIEREMVGFS
EAMHILGVRF TPKALMSRAK AGFLSENSIV LNLPGSTKGV KQNLEMLLPL VKHALKMAKG
EGH
//