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Database: UniProt
Entry: A0A1D6HB30_MAIZE
LinkDB: A0A1D6HB30_MAIZE
Original site: A0A1D6HB30_MAIZE 
ID   A0A1D6HB30_MAIZE        Unreviewed;       503 AA.
AC   A0A1D6HB30;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Bifunctional riboflavin biosynthesis protein RIBA 1 chloroplastic {ECO:0000313|EMBL:AQK71907.1};
GN   Name=100304324 {ECO:0000313|EnsemblPlants:Zm00001eb244650_P004};
GN   ORFNames=ZEAMMB73_Zm00001d016902 {ECO:0000313|EMBL:AQK71907.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK71907.1};
RN   [1] {ECO:0000313|EnsemblPlants:Zm00001eb244650_P004, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb244650_P004,
RC   ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [2] {ECO:0000313|EMBL:AQK71907.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK71907.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb244650_P004}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb244650_P004};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) 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   EMBL; CM000781; AQK71907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6HB30; -.
DR   EnsemblPlants; Zm00001eb244650_T004; Zm00001eb244650_P004; Zm00001eb244650.
DR   Gramene; Zm00001eb244650_T004; Zm00001eb244650_P004; Zm00001eb244650.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; A0A1D6HB30; baseline and differential.
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_00180; RibB; 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   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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6HB30};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT   DOMAIN          344..476
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
SQ   SEQUENCE   503 AA;  54593 MW;  007DC134B50E8F35 CRC64;
     MPSIAPPSSS VAALTRQPVQ FFKGCSVSKE TKGPVRSFFT ANSKSTKVKS AGLKVASSFK
     NDGGYPAGGV SWKDDTLLPK STTIRGQDHS VADPVLPMDS MITPEILSAN VERVIDMFAD
     DDTDTELDLD SPTEGFTSIA EAIEDIQQGK LVIVVDDESR ENEGDLIMAA SLVTPEAMAF
     IVRHGTGIVC VSMKEDDLER LSLPLMVTTK ENEEKLCTAF TVTVDAKEGT TTGVSAKDRA
     KTVMTLASPD SKPEDLNRPG HIFPLKYREG GVLKRAGHTE ASVDLAMLAG LPPVAVLCEI
     VDDADGSMAR LPKLRVFAEK ENLKIISIAD LIRYRRKRDR LIERASVARL PLKWGNVHAY
     CYKSVIDGIE HIAMVKGDIG DGQDILVRVH SECLTGDIFG SARCDCGDQL AMAMEMIEKA
     GRGVLVYLRG HEGRGIGLGH KLRAYNLQDD GRDTVEANEE LGLPVDSREY GIGAQVRLNY
     LSSYRGTFLH NSSFLLKSAC IGK
//
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