ID A0A067EET7_CITSI Unreviewed; 564 AA.
AC A0A067EET7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GTP cyclohydrolase II domain-containing protein {ECO:0000259|Pfam:PF00925};
GN ORFNames=CISIN_1g008469mg {ECO:0000313|EMBL:KDO49692.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO49692.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO49692.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK785104; KDO49692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067EET7; -.
DR STRING; 2711.A0A067EET7; -.
DR PaxDb; 2711-XP_006492616-1; -.
DR eggNOG; KOG1284; Eukaryota.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; TIGR00505; ribA; 1.
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:UP000027120};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 346..510
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 564 AA; 60573 MW; B5AD81F366395116 CRC64;
MAASLNISSP STSALSSPPA CRNVKFVSGF PSTKSLLANG HSSYLAFVKL ATKSSISIKG
VGKTRATLIS GEGDLLAYPN GNNLVAESTG ADDQLVGIEL QPDAIAFGAL AADTAPTTFG
FSSDDDEFDL DSPTEGFSSI PEAIEDIRQG KFVVVVDDED RENEGDLIMA AQLATPEAMA
FIVKHGTGIV CVSMKGEDLE RLDLPLMVAQ KENDEKLCTA FTVTVDAKHG TTTGVSARDR
ATTVLTLASR DSKPGDFNRP GHIFPLKYRE GGVLKRAGHT EASVDLAVLA GFDPAAVLCE
VVDDDGSMAR LPKLREFAKR ENLKIISIAD LIRYRRKRDK LVDRSSAARI PTMWGPFTAY
CYRSILDGIE HIAMVKGDIG DGQDILVRVH SECLTGDIFG SARCDCGDQL ALAMQQIEAA
GRGVLVYLRG HEGRGIGLGH KLRAYNLQDD GRDTVEANEE LGLPVDSREY GIGAQMLRDL
GVRTMKLMTN NPSKYVGLKG YGLAVAGRVP LITPIKKENK RYLETKRAKM GHIYGLESNG
RLTNLINGNG KPSIKSSSDT VSDS
//
