ID Q0TWL1_PHANO Unreviewed; 395 AA.
AC Q0TWL1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=SNOG_16138 {ECO:0000313|EMBL:EAT76510.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT76510.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445367; EAT76510.1; -; Genomic_DNA.
DR RefSeq; XP_001806265.1; XM_001806213.1.
DR AlphaFoldDB; Q0TWL1; -.
DR STRING; 321614.Q0TWL1; -.
DR EnsemblFungi; SNOT_16138; SNOT_16138; SNOG_16138.
DR GeneID; 5983195; -.
DR KEGG; pno:SNOG_16138; -.
DR VEuPathDB; FungiDB:JI435_161380; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_2_4_1; -.
DR InParanoid; Q0TWL1; -.
DR OMA; RLPNVEC; -.
DR OrthoDB; 1328905at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0019238; F:cyclohydrolase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000001055};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 225..354
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 395 AA; 43139 MW; 22D981F37C7666E3 CRC64;
MPSLPSHASP GLPPLYSPDP NRRDPFDDHN SDEDLGKSAI RNNAPNAPQE PPPSIISPAF
TPPATPGTST PSHPRPPRSI PVDTSTASQT ERPELLEKLP DVACEVRARI PTTTGHEMWL
HVYRNSVDTK EHLAIVFGGK IRSRSLDAER PGETELDRMT RGAYVGRLYP GRTSSRVEQI
KRSEGVPSKR IPDKIPENTN GMPSPSSPAS SENGDAQSIT SSDLPLVRIH SECYTGETVW
SARCDCGEQL DEAARLMADP TLSPSGGAII YLRQEGRGIG LGEKLKAYNL QDLGNDTYEA
NILLRHPADA RSYGLATAML MDLGLGGERG IRLLTNNPDK VHAVEGPGRE VVVRERVAMV
PLAWKTGGER GIKSDEVEKY LSTKIEKFKH MLDQK
//
