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Database: UniProt
Entry: K3VCV6_FUSPC
LinkDB: K3VCV6_FUSPC
Original site: K3VCV6_FUSPC 
ID   K3VCV6_FUSPC            Unreviewed;       390 AA.
AC   K3VCV6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN   ORFNames=FPSE_08290 {ECO:0000313|EMBL:EKJ71549.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ71549.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ71549.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ71549.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKJ71549.1}.
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DR   EMBL; AFNW01000285; EKJ71549.1; -; Genomic_DNA.
DR   RefSeq; XP_009259683.1; XM_009261408.1.
DR   AlphaFoldDB; K3VCV6; -.
DR   EnsemblFungi; EKJ71549; EKJ71549; FPSE_08290.
DR   GeneID; 20366908; -.
DR   KEGG; fpu:FPSE_08290; -.
DR   eggNOG; KOG1284; Eukaryota.
DR   HOGENOM; CLU_020273_2_4_1; -.
DR   OrthoDB; 1328905at2759; -.
DR   Proteomes; UP000007978; Chromosome 2.
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   NCBIfam; TIGR00505; ribA; 1.
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:UP000007978};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT   DOMAIN          132..345
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..85
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  41659 MW;  16D42911362A601D CRC64;
     MPSDATPGSP AGSNSALPPF YSPKTEPADA STPAHHHNDT LEQSIDSLSL SPAPSTPASA
     PVSAHPDPET PIGLEPPPSL LSPSFTPPST PGTSTPTTAG LRGVPVDSSI PSGGCGSKRP
     KLLPTLPEVE CIVRARIPTV AGTEMFLHLY TNNVDNKEHL AIVFGKNIRS KSLDAVREGE
     TEMDRMVRGA YTGRLFPGRT TSGIGPATPQ EEQPPQPSDQ PPLVRIHSEC YTGETAWSAR
     CDCGEQLDEA ARLMSLPGNK AGGIIIYLRQ EGRGIGLGEK LKAYNLQDLG SDTVEANLLL
     RHPADARSYG LATAMLLDLG HPEVRLLTNN PDKIRAVEGP NREVVVKERV AMVPLSWKGR
     GGFRSQEVEG YLKTKIEKMG HMLDMASVPR
//
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