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Database: UniProt
Entry: A0A0C9YFH1_9AGAR
LinkDB: A0A0C9YFH1_9AGAR
Original site: A0A0C9YFH1_9AGAR 
ID   A0A0C9YFH1_9AGAR        Unreviewed;       503 AA.
AC   A0A0C9YFH1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN   ORFNames=K443DRAFT_674113 {ECO:0000313|EMBL:KIK06828.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK06828.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIK06828.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK06828.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC         pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00029293};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005104}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC       {ECO:0000256|ARBA:ARBA00008131}.
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DR   EMBL; KN838551; KIK06828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9YFH1; -.
DR   STRING; 1095629.A0A0C9YFH1; -.
DR   HOGENOM; CLU_020273_2_4_1; -.
DR   OrthoDB; 1328905at2759; -.
DR   Proteomes; UP000054477; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   PANTHER; PTHR21327:SF29; GTP CYCLOHYDROLASE-2; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT   DOMAIN          275..424
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          80..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  55340 MW;  08BFAA79CEAED23F CRC64;
     MRHHQSIDPD ADAALLDILT GPTPQAAAKS FARRDAALDP LLIAAAAASG PHVTRNHYHH
     DFFPGVMLPK AEGSWDWTKW TGDSSSRPER KRFAYVSRQA PRRQRLQPST AEEGKENDYP
     RGMDPLKPAD NLPPVPKKRR SSLASPINSE GRNWSKALSS PDSPPKPDAT PVEVKCMART
     RIPTPHGPVF LHLYHSNRDA KEHLAIVIDP AQTSDDALAA PPIRSRSLDA VWSETETEAE
     RIIRGAYIGR LSPTLQRPSN PSCHHSASIP VMTGVPSPLI RIHSECFTGE TVGSMRCDCG
     EQLDEAIRQI SQPIALPATS SRKSTAIPGR GAIIYLRQEG RGIGLLSKIR AYNLQDMGHD
     TVTANLMLGH KADERGYEIA GAILRDLGLG SDHAGLEGVR VLTNNPDKVE ALQRENIRVV
     ERVPMIPRSW QNRKPQADAK SLPGDPLSYI PRKQKEMSRA SGATLIGGGT VYGEDLDKYL
     RTKVLRMGHM LPLWMESPET PLY
//
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