ID G0RUL7_HYPJQ Unreviewed; 372 AA.
AC G0RUL7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=TRIREDRAFT_123805 {ECO:0000313|EMBL:EGR45094.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR45094.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR45094.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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; GL985082; EGR45094.1; -; Genomic_DNA.
DR RefSeq; XP_006969004.1; XM_006968942.1.
DR AlphaFoldDB; G0RUL7; -.
DR STRING; 431241.G0RUL7; -.
DR EnsemblFungi; EGR45094; EGR45094; TRIREDRAFT_123805.
DR GeneID; 18483740; -.
DR KEGG; tre:TRIREDRAFT_123805; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_123805; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_2_4_1; -.
DR OrthoDB; 1328905at2759; -.
DR Proteomes; UP000008984; 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 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; 2.
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:UP000008984};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 199..327
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 40168 MW; A15EB80E98E6B147 CRC64;
MTSDASFGAG DTAQLPSFYS PRTAAVDPPR SRDGQPIDDL SLSQSSHINS PKTQPPPPSL
LSPAFTPPAT PGDQTPTTAG LRGIPVDSSI ASGGCGSKKP KLLETLPEVQ CVVRARIPTV
NGTEMFLHLY TNNVDNKEHL AIVFGNHIRS KSLDAPREGE TEMDRMIRGA YTGRLYPGRT
TSGMGGPSSE AESQRGQYSS QDPPLVRIHS ECYTGETAWS ARCDCGEQLD EAARLMSLPG
NKAGGIIIYL RQEGRGIGLG EKLKAYNLQD LGSDTVEANL LLRHPADARS YGLATAMLMD
LGQKEVRLLT NNPDKIRAIE GPNREIVVKE RVAMVPLSWK GKGGFRSQEV EGYLKTKIEK
MGHMLDMAGL PQ
//
