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Database: UniProt
Entry: F0S3P2_DESTD
LinkDB: F0S3P2_DESTD
Original site: F0S3P2_DESTD 
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
//
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