ID   M8CSH8_AEGTA            Unreviewed;       691 AA.
AC   M8CSH8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
OS   Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT26656};
RN   [1] {ECO:0000313|EnsemblPlants:EMT26656}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004853}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family.
CC       {ECO:0000256|RuleBase:RU000660}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000256|ARBA:ARBA00008976}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000256|ARBA:ARBA00005520}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; M8CSH8; -.
DR   EnsemblPlants; EMT26656; EMT26656; F775_30965.
DR   UniPathway; UPA00275; UER00400.
DR   ExpressionAtlas; M8CSH8; baseline.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   Gene3D; 3.90.1030.10; Ribosomal protein L17; 1.
DR   HAMAP; MF_00179; RibA; 1.
DR   HAMAP; MF_01283; RibBA; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   InterPro; IPR016299; Riboflavin_synth_RibBA.
DR   InterPro; IPR000456; Ribosomal_bL17.
DR   InterPro; IPR036373; Ribosomal_bL17_sf.
DR   NCBIfam; TIGR00059; L17; 1.
DR   NCBIfam; TIGR00505; ribA; 1.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   PANTHER; PTHR21327:SF29; GTP CYCLOHYDROLASE-2; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   Pfam; PF01196; Ribosomal_L17; 1.
DR   SUPFAM; SSF64263; Prokaryotic ribosomal protein L17; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU000660};
KW   Ribosomal protein {ECO:0000256|RuleBase:RU000660}.
FT   DOMAIN          476..645
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
SQ   SEQUENCE   691 AA;  75342 MW;  D8F26AFB83F25C39 CRC64;
     MGNFRKLGRH AAHRVSMLRT MVSQLVKHER IETTVAKAKE VRRKADQMVQ LGKDGTLDAA
     RRASAFVRGD DVVHKLFTEL AYRYKFVDRE NELREAKPAT PPPPQRAPLD PWTKSHASQH
     SETCGQFGYT LRGFFFCYPH DQISPSDRLR VIAAVQAIEM DCVLLSSHLS SHATVNARLQ
     QCSVSLNSIG FAVIRKGCLR LRCYAIGDAG RRNDPLDENK NGPISQELNG SSASFTTVGA
     EITQETGDFF SSDAEGDPDK PTEGFSSIED AINSLREGKF VIAVDDEKGD NEGDLIMAAD
     QASPESIAFM IRNGSGIISV GMKEEDLERL MLPMMSPVTE IGDISATAST VTVDARVGIS
     TGVSAADRAK TILALASPDS KPSDLRRPGH IFPLKYRNGG VLKRAGHTEA SVDLVALAGL
     RPVSVLSSII DPKDGSMAST PALKQMALEH DIPIVSIADL IRYRRKREKL VELIAVSRLP
     TKWGLFRAYC YQSKLDGTEH IAVTKFEANV QGDIGDGEDV LVRVHSECLT GDILGSARCD
     CGEQLDLAMQ LIEKAGRGVL VYLRGHEGRG IGLGQKLRAY NLQDQGSDTV EANVELGLAI
     DSREYGIGAQ ILRDIGVRTM RLMTNNPAKF VGLKGYGLAV VGRVPVISPI TKENQKYLET
     KRTKMGHLYG SDLPGGLLKE FLNPTEDNAT N
//