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Database: UniProt
Entry: V7CPE5_PHAVU
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Original site: V7CPE5_PHAVU 
ID   V7CPE5_PHAVU            Unreviewed;       532 AA.
AC   V7CPE5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN   ORFNames=PHAVU_002G210900g {ECO:0000313|EMBL:ESW31120.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW31120.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
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: 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; CM002289; ESW31120.1; -; Genomic_DNA.
DR   RefSeq; XP_007159126.1; XM_007159064.1.
DR   AlphaFoldDB; V7CPE5; -.
DR   STRING; 3885.V7CPE5; -.
DR   EnsemblPlants; ESW31120; ESW31120; PHAVU_002G210900g.
DR   GeneID; 18638641; -.
DR   Gramene; ESW31120; ESW31120; PHAVU_002G210900g.
DR   KEGG; pvu:PHAVU_002G210900g; -.
DR   eggNOG; KOG1284; Eukaryota.
DR   OMA; HITMVKG; -.
DR   OrthoDB; 5489599at2759; -.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000000226; 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; TIGR00505; ribA; 1.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF37; GTP CYCLOHYDROLASE II; 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:UP000000226};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT   DOMAIN          323..486
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          510..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  57264 MW;  7D84AAAF18A03B98 CRC64;
     MASSISLSTP FYRPSVCKQL KLFTGLHKFS LSGHGSDLAF VQLNSSATFR IKATLTSGRG
     VLGSYPNSNG VGAEGQRDVA AFGTPGIDTA VPAGSGFSDD DDEYDFDSPT EGFASVPEAI
     EDIRNGKMVV VVDDEDRENE GDLIMAAELA TPEAMAFIVK HGTGIVCISM KEEDLERLDL
     PLMVNSQYND EKLRTAFTVT VDAKHGTTTG VSARDRATTV LALASKDSKP SDFNRPGHIF
     PLKYREGGVL KRAGHTEASV DLAILAGLNP AAVLCEIVDD DGSMARLPKL RQFAERENLK
     IVSIADLIRY RRKRDKLVEP AGSAVIPTTW GPFTANCYRS LLDGIEHITM VKGDISDGHD
     VLVRVHSECL TGDIFGSARC DCGNQLSIAM QQIETAGRGV LVYLRGHEGR GIGLGHKLRA
     YNLQDDGRDT VEANEELGLP VDSREYGIGA QILRDLGVRS MKLMTNNPAK YVGLKGYGLT
     ISGRIPLLSL VTKENKRYLE TKRVKMGHVY GLPESGNGKA GSGDDSNAAP GL
//
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