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Database: UniProt
Entry: A0A1Q3B667_CEPFO
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ID   A0A1Q3B667_CEPFO        Unreviewed;       590 AA.
AC   A0A1Q3B667;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN   ORFNames=CFOL_v3_06782 {ECO:0000313|EMBL:GAV63262.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV63262.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) 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; 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAV63262.1}.
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DR   EMBL; BDDD01000301; GAV63262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3B667; -.
DR   STRING; 3775.A0A1Q3B667; -.
DR   InParanoid; A0A1Q3B667; -.
DR   OrthoDB; 5489599at2759; -.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000187406; Unassembled WGS sequence.
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; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   PANTHER; PTHR21327:SF41; MONOFUNCTIONAL RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBA 2, CHLOROPLASTIC; 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:UP000187406};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..590
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012885317"
FT   DOMAIN          374..537
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   REGION          561..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  64435 MW;  9D732272F54386EC CRC64;
     MWWCCQGPKP NKLHLVISLS LSLSLSNTLL KEMTSFNLYS SSSVISPSLV YNGLHCVVPL
     ITNGSTSVLV SSTLTRKWLF SYKGVSTARA TLVSGEGDLI SFPNNNRAPR QDTFVDKQLN
     QPGGIEIQPD AIGFGTLSAE VTPTISSFHT GNDEYDLDRP TEGFASVEEA IEDIRQGKMV
     IVVDDEDREN EGDLIMAASL VTPEAMSFIV KHGTGIVCVS MKDEDLERLE LPLMVTLKEN
     EEKLCTAFTV SVDAKRGTTT GVSARDRAAT VKALACRDSK AEDFNRPGHV FPLKYREGGV
     LKRAGHTEAS VDLAVLAGLD PVAVLCEIVD DDGSMARLPK LRQFALEENL KIISIADLIR
     FRRKRDRLVE LAAAAPIPTM WGPFKAYCYR SLLDGIEHIA MVKGEVEDGQ DILVRVHSEC
     LTGDIFGSAR CDCGNQLALA MKQIKAAGRG VLVYLRGHEG RGIGLGHKLR AYNLQDDGRD
     TVEANEELGL PVDSREYGIG AQILRDLGVR TMRLMTNNPA KYIGLKGYGL AIAGRVPLLT
     PITKENMRYI ETKRDKLGHI YESDSNGHVN GSMNDNSSSM DNPSNGVSET
//
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