ID A0A0D3F6Q1_9ORYZ Unreviewed; 542 AA.
AC A0A0D3F6Q1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=GTP cyclohydrolase II domain-containing protein {ECO:0000259|Pfam:PF00925};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G21420.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART02G21420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G21420.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART02G21420.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004904}.
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: 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}.
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DR AlphaFoldDB; A0A0D3F6Q1; -.
DR STRING; 65489.A0A0D3F6Q1; -.
DR PaxDb; 65489-OBART02G21420-1; -.
DR EnsemblPlants; OBART02G21420.1; OBART02G21420.1; OBART02G21420.
DR Gramene; OBART02G21420.1; OBART02G21420.1; OBART02G21420.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_1_0_1; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000026960; Chromosome 2.
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:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
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 HAMAP; MF_00179; RibA; 1.
DR HAMAP; MF_00180; RibB; 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 NCBIfam; TIGR00506; ribB; 1.
DR PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 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 Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 345..498
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 70..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 58372 MW; 5FD48274E879F926 CRC64;
MASISPTSSS VAALRGHPVQ FVKGGAVSKE AKGSISFSPV ANSNNANVKF TGLRVAASLK
RDGAFPGDGY SGNDNTVLPK STSVRGQDYP TADSVLPTES VIVPEISNAG LKCVADMFSD
EDKDTEQDLD SPTEGFSSIS EAIKDIQQGK LVIVVDDESR ENEGDLIMAA SLVTPEAMAF
VVRYGTGIVC VSMKEEDLER LNLPLMVATK ENEEKLCTAF TVTVDAKEGT TTGVSATDRA
KTVMTLASPD SKPEDFNRPG HIFPLKYREG GVLKRAGHTE ASVDLAMLAG LPPAAVLCEI
VDEDGSMARL PKLRVFAERE NLKIVSIADL IRYRRKRDRL VERSSVARLP LRWGNVRAYC
YRSVIDGIEH IAMVKGEIGD GQGVLVRVHS ECLTGDIFGS ARCDCGDQLA MAMEMIEKAG
RGVLVYLRGH EGRGIGLGHK LRAYNLQDDG RDTVEANEDL GLPILRDLGV RSMKLMTNNP
AKYGGLKGYG LSIVGRVPLV TPITSENRRY LETKRTKMGH VYGLANGQAS HQTGSNGAKG
EH
//
